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Manganese in PDB 6zee: Structure of PP1(7-300) Bound to PHACTR1 (507-580) at PH8.4

Enzymatic activity of Structure of PP1(7-300) Bound to PHACTR1 (507-580) at PH8.4

All present enzymatic activity of Structure of PP1(7-300) Bound to PHACTR1 (507-580) at PH8.4:
3.1.3.16;

Protein crystallography data

The structure of Structure of PP1(7-300) Bound to PHACTR1 (507-580) at PH8.4, PDB code: 6zee was solved by S.Mouilleron, R.Treisman, R.Fedoryshchak, R.Lee, A.M.Butler, M.Prechova, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 119.25 / 1.90
Space group P 65
Cell size a, b, c (Å), α, β, γ (°) 137.695, 137.695, 238.793, 90.00, 90.00, 120.00
R / Rfree (%) 23.6 / 26.8

Manganese Binding Sites:

Pages:

>>> Page 1 <<< Page 2, Binding sites: 11 - 12;

Binding sites:

The binding sites of Manganese atom in the Structure of PP1(7-300) Bound to PHACTR1 (507-580) at PH8.4 (pdb code 6zee). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 12 binding sites of Manganese where determined in the Structure of PP1(7-300) Bound to PHACTR1 (507-580) at PH8.4, PDB code: 6zee:
Jump to Manganese binding site number: 1; 2; 3; 4; 5; 6; 7; 8; 9; 10;

Manganese binding site 1 out of 12 in 6zee

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Manganese binding site 1 out of 12 in the Structure of PP1(7-300) Bound to PHACTR1 (507-580) at PH8.4


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Structure of PP1(7-300) Bound to PHACTR1 (507-580) at PH8.4 within 5.0Å range:
probe atom residue distance (Å) B Occ
P:Mn501

b:33.8
occ:1.00
HD1 P:HIS248 1.7 51.0 1.0
O2 P:SO4512 2.0 39.8 1.0
OD1 P:ASP92 2.2 36.7 1.0
OD1 P:ASN124 2.2 39.5 1.0
NE2 P:HIS173 2.3 37.1 1.0
ND1 P:HIS248 2.5 42.4 1.0
HE1 P:HIS248 2.9 52.6 1.0
CE1 P:HIS248 3.0 43.7 1.0
HD21 P:ASN124 3.0 46.6 1.0
MN P:MN502 3.1 43.7 1.0
HA P:HIS248 3.1 53.7 1.0
CE1 P:HIS173 3.1 37.3 1.0
CG P:ASN124 3.2 38.4 1.0
S P:SO4512 3.3 42.4 1.0
CG P:ASP92 3.3 37.1 1.0
HE1 P:HIS173 3.3 44.9 1.0
HD2 P:HIS125 3.3 46.9 1.0
CD2 P:HIS173 3.3 38.7 1.0
ND2 P:ASN124 3.5 39.0 1.0
O1 P:SO4512 3.5 49.8 1.0
HD2 P:HIS173 3.5 46.6 1.0
OD2 P:ASP92 3.7 36.9 1.0
CG P:HIS248 3.7 42.3 1.0
O4 P:SO4512 3.9 42.9 1.0
H P:ASN124 4.0 43.9 1.0
OD2 P:ASP64 4.0 39.1 1.0
CA P:HIS248 4.0 44.6 1.0
CD2 P:HIS125 4.1 38.9 1.0
O P:HIS248 4.2 45.1 1.0
NE2 P:HIS248 4.3 43.1 1.0
HE2 P:HIS125 4.3 47.0 1.0
ND1 P:HIS173 4.3 36.1 1.0
HD22 P:ASN124 4.3 46.6 1.0
CB P:HIS248 4.3 41.7 1.0
O3 P:SO4512 4.4 38.1 1.0
HH12 P:ARG221 4.4 51.9 1.0
CG P:HIS173 4.4 36.6 1.0
HB2 P:HIS248 4.5 50.2 1.0
CB P:ASP92 4.5 35.5 1.0
CB P:ASN124 4.5 39.0 1.0
NE2 P:HIS125 4.6 39.0 1.0
HB2 P:ASP92 4.6 42.5 1.0
C P:HIS248 4.6 43.5 1.0
CD2 P:HIS248 4.6 43.4 1.0
N P:ASN124 4.7 37.2 1.0
HB3 P:ASN124 4.7 47.0 1.0
NH1 P:ARG221 4.8 43.2 1.0
HB3 P:ASP92 4.8 42.5 1.0
HE1 P:HIS66 4.8 48.0 1.0
NE2 P:HIS66 4.8 41.1 1.0
H P:HIS125 4.8 43.8 1.0
O P:LEU205 4.8 41.3 1.0
HH22 P:ARG221 4.9 52.1 1.0
HE2 P:HIS248 4.9 51.9 1.0
H P:HIS248 5.0 47.4 1.0

Manganese binding site 2 out of 12 in 6zee

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Manganese binding site 2 out of 12 in the Structure of PP1(7-300) Bound to PHACTR1 (507-580) at PH8.4


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of Structure of PP1(7-300) Bound to PHACTR1 (507-580) at PH8.4 within 5.0Å range:
probe atom residue distance (Å) B Occ
P:Mn502

b:43.7
occ:1.00
O1 P:SO4512 2.1 49.8 1.0
NE2 P:HIS66 2.1 41.1 1.0
OD1 P:ASP92 2.4 36.7 1.0
OD2 P:ASP64 2.4 39.1 1.0
O P:HOH623 2.5 40.8 1.0
CE1 P:HIS66 2.9 39.9 1.0
HE1 P:HIS66 3.0 48.0 1.0
MN P:MN501 3.1 33.8 1.0
S P:SO4512 3.2 42.4 1.0
CD2 P:HIS66 3.2 37.6 1.0
O2 P:SO4512 3.3 39.8 1.0
HH22 P:ARG96 3.3 54.7 1.0
CG P:ASP92 3.3 37.1 1.0
HB3 P:ASP92 3.4 42.5 1.0
HD2 P:HIS66 3.4 45.2 1.0
CG P:ASP64 3.6 37.1 1.0
HD2 P:HIS125 3.8 46.9 1.0
CB P:ASP92 3.8 35.5 1.0
HE1 P:HIS173 3.8 44.9 1.0
HH21 P:ARG96 3.9 54.7 1.0
HB3 P:ASP64 3.9 44.8 1.0
HB2 P:ASP92 3.9 42.5 1.0
NH2 P:ARG96 3.9 45.5 1.0
O4 P:SO4512 3.9 42.9 1.0
HH P:TYR272 4.0 50.6 1.0
HE2 P:HIS125 4.0 47.0 1.0
O P:HOH667 4.1 42.0 1.0
HA P:HIS248 4.1 53.7 1.0
ND1 P:HIS66 4.1 40.1 1.0
HD1 P:HIS248 4.1 51.0 1.0
HE1 P:PHE267 4.1 46.0 1.0
CD2 P:HIS125 4.1 38.9 1.0
CG P:HIS66 4.2 37.6 1.0
NE2 P:HIS125 4.3 39.0 1.0
OH P:TYR272 4.3 42.0 1.0
O3 P:SO4512 4.3 38.1 1.0
CB P:ASP64 4.3 37.2 1.0
OD2 P:ASP92 4.4 36.9 1.0
CE1 P:HIS173 4.4 37.3 1.0
NE2 P:HIS173 4.4 37.1 1.0
OD1 P:ASP64 4.6 35.7 1.0
O P:HIS248 4.6 45.1 1.0
HB2 P:ASP64 4.7 44.8 1.0
OD1 P:ASN124 4.8 39.5 1.0
HD1 P:HIS66 4.9 48.3 1.0
ND1 P:HIS248 4.9 42.4 1.0
CA P:HIS248 5.0 44.6 1.0
CE1 P:PHE267 5.0 38.5 1.0
HD21 P:ASN124 5.0 46.6 1.0

Manganese binding site 3 out of 12 in 6zee

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Manganese binding site 3 out of 12 in the Structure of PP1(7-300) Bound to PHACTR1 (507-580) at PH8.4


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 3 of Structure of PP1(7-300) Bound to PHACTR1 (507-580) at PH8.4 within 5.0Å range:
probe atom residue distance (Å) B Occ
Q:Mn501

b:39.5
occ:1.00
OD1 Q:ASN124 2.2 48.4 1.0
NE2 Q:HIS173 2.2 46.4 1.0
OD2 Q:ASP92 2.3 49.9 1.0
O4 Q:SO4508 2.4 44.5 1.0
ND1 Q:HIS248 2.5 44.3 1.0
O Q:HOH601 2.5 46.2 1.0
HE1 Q:HIS248 2.8 51.4 1.0
CE1 Q:HIS248 3.0 42.7 1.0
MN Q:MN502 3.0 49.1 1.0
CE1 Q:HIS173 3.1 43.6 1.0
HA Q:HIS248 3.1 51.7 1.0
HD21 Q:ASN124 3.1 56.6 1.0
CG Q:ASN124 3.2 48.0 1.0
CG Q:ASP92 3.2 50.1 1.0
HE1 Q:HIS173 3.2 52.5 1.0
CD2 Q:HIS173 3.3 45.5 1.0
HD2 Q:HIS125 3.3 58.7 1.0
S Q:SO4508 3.4 42.6 1.0
HD2 Q:HIS173 3.5 54.8 1.0
ND2 Q:ASN124 3.5 47.8 1.0
OD1 Q:ASP92 3.5 49.8 1.0
O1 Q:SO4508 3.6 49.0 1.0
CG Q:HIS248 3.7 42.8 1.0
O2 Q:SO4508 3.7 40.4 1.0
H Q:ASN124 3.9 57.3 1.0
CA Q:HIS248 4.0 43.0 1.0
CD2 Q:HIS125 4.1 49.6 1.0
OD2 Q:ASP64 4.2 47.6 1.0
NE2 Q:HIS248 4.3 41.3 1.0
ND1 Q:HIS173 4.3 43.6 1.0
O Q:HIS248 4.3 46.8 1.0
CB Q:HIS248 4.3 41.6 1.0
HE2 Q:HIS125 4.4 58.8 1.0
CG Q:HIS173 4.4 43.3 1.0
HD22 Q:ASN124 4.4 56.6 1.0
CB Q:ASP92 4.5 50.9 1.0
HB2 Q:HIS248 4.5 50.1 1.0
HB2 Q:ASP92 4.5 60.2 1.0
CB Q:ASN124 4.5 47.6 1.0
HH12 Q:ARG221 4.5 48.6 1.0
CD2 Q:HIS248 4.6 40.4 1.0
NE2 Q:HIS125 4.6 49.5 1.0
O3 Q:SO4508 4.6 44.0 1.0
N Q:ASN124 4.7 48.4 1.0
HB3 Q:ASN124 4.7 56.3 1.0
C Q:HIS248 4.7 44.9 1.0
O Q:LEU205 4.7 42.1 1.0
HB3 Q:ASP92 4.8 60.2 1.0
H Q:HIS125 4.8 58.1 1.0
HE1 Q:HIS66 4.8 56.6 1.0
NE2 Q:HIS66 4.8 49.6 1.0
HE2 Q:HIS248 4.9 49.7 1.0
H Q:HIS248 4.9 52.6 1.0
NH1 Q:ARG221 5.0 40.4 1.0

Manganese binding site 4 out of 12 in 6zee

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Manganese binding site 4 out of 12 in the Structure of PP1(7-300) Bound to PHACTR1 (507-580) at PH8.4


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 4 of Structure of PP1(7-300) Bound to PHACTR1 (507-580) at PH8.4 within 5.0Å range:
probe atom residue distance (Å) B Occ
Q:Mn502

b:49.1
occ:1.00
NE2 Q:HIS66 2.0 49.6 1.0
OD2 Q:ASP92 2.1 49.9 1.0
O1 Q:SO4508 2.2 49.0 1.0
OD2 Q:ASP64 2.5 47.6 1.0
O Q:HOH601 2.7 46.2 1.0
CE1 Q:HIS66 2.9 47.0 1.0
HE1 Q:HIS66 3.0 56.6 1.0
MN Q:MN501 3.0 39.5 1.0
CD2 Q:HIS66 3.2 47.4 1.0
S Q:SO4508 3.2 42.6 1.0
CG Q:ASP92 3.2 50.1 1.0
HB3 Q:ASP92 3.3 60.2 1.0
HD2 Q:HIS66 3.4 57.1 1.0
O4 Q:SO4508 3.4 44.5 1.0
O2 Q:SO4508 3.6 40.4 1.0
CG Q:ASP64 3.7 45.7 1.0
CB Q:ASP92 3.7 50.9 1.0
HD2 Q:HIS125 3.7 58.7 1.0
HE1 Q:HIS173 3.7 52.5 1.0
HB2 Q:ASP92 3.8 60.2 1.0
HB3 Q:ASP64 3.9 57.2 1.0
HE2 Q:HIS125 4.0 58.8 1.0
HA Q:HIS248 4.0 51.7 1.0
ND1 Q:HIS66 4.1 52.3 1.0
CD2 Q:HIS125 4.1 49.6 1.0
HE Q:ARG96 4.2 68.1 1.0
HE1 Q:PHE267 4.2 53.7 1.0
CG Q:HIS66 4.2 47.3 1.0
NE2 Q:HIS125 4.2 49.5 1.0
HH Q:TYR272 4.3 62.9 1.0
OH Q:TYR272 4.3 53.0 1.0
OD1 Q:ASP92 4.3 49.8 1.0
CB Q:ASP64 4.3 47.5 1.0
NE2 Q:HIS173 4.4 46.4 1.0
CE1 Q:HIS173 4.4 43.6 1.0
O Q:HOH649 4.4 45.3 1.0
O3 Q:SO4508 4.5 44.0 1.0
O Q:HIS248 4.5 46.8 1.0
OD1 Q:ASP64 4.6 44.2 1.0
OD1 Q:ASN124 4.7 48.4 1.0
HB2 Q:ASP64 4.8 57.2 1.0
HD1 Q:HIS66 4.8 62.9 1.0
ND1 Q:HIS248 4.8 44.3 1.0
CA Q:HIS248 4.9 43.0 1.0
HH21 Q:ARG96 5.0 65.6 1.0
C Q:HIS248 5.0 44.9 1.0

Manganese binding site 5 out of 12 in 6zee

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Manganese binding site 5 out of 12 in the Structure of PP1(7-300) Bound to PHACTR1 (507-580) at PH8.4


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 5 of Structure of PP1(7-300) Bound to PHACTR1 (507-580) at PH8.4 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mn501

b:36.2
occ:1.00
O1 B:SO4516 2.2 28.4 1.0
O B:HOH632 2.2 27.4 1.0
OD1 B:ASN124 2.2 26.1 1.0
OD1 B:ASP92 2.3 25.9 1.0
NE2 B:HIS173 2.3 25.9 1.0
ND1 B:HIS248 2.4 26.9 1.0
HE1 B:HIS248 2.8 33.0 1.0
CE1 B:HIS248 2.9 27.4 1.0
HA B:HIS248 3.0 32.5 1.0
MN B:MN502 3.1 37.8 1.0
HD21 B:ASN124 3.1 30.6 1.0
CG B:ASN124 3.1 25.9 1.0
CG B:ASP92 3.2 26.8 1.0
CE1 B:HIS173 3.2 25.7 1.0
CD2 B:HIS173 3.3 25.7 1.0
S B:SO4516 3.3 32.6 1.0
HE1 B:HIS173 3.4 31.0 1.0
HD2 B:HIS125 3.5 32.8 1.0
HD2 B:HIS173 3.5 31.0 1.0
ND2 B:ASN124 3.5 25.3 1.0
OD2 B:ASP92 3.5 23.5 1.0
O2 B:SO4516 3.6 31.4 1.0
CG B:HIS248 3.6 26.4 1.0
O4 B:SO4516 3.9 31.8 1.0
H B:ASN124 3.9 29.9 1.0
CA B:HIS248 3.9 26.9 1.0
OD2 B:ASP64 4.0 26.8 1.0
O B:HIS248 4.1 29.6 1.0
NE2 B:HIS248 4.2 26.4 1.0
CB B:HIS248 4.2 26.4 1.0
CD2 B:HIS125 4.3 27.2 1.0
HD22 B:ASN124 4.3 30.6 1.0
ND1 B:HIS173 4.4 25.2 1.0
HB2 B:HIS248 4.4 31.9 1.0
CB B:ASP92 4.4 24.9 1.0
CG B:HIS173 4.5 24.9 1.0
HB2 B:ASP92 4.5 30.0 1.0
C B:HIS248 4.5 28.3 1.0
CB B:ASN124 4.5 25.9 1.0
O3 B:SO4516 4.5 31.4 1.0
CD2 B:HIS248 4.5 26.9 1.0
HH12 B:ARG221 4.5 37.2 1.0
N B:ASN124 4.6 24.8 1.0
HB3 B:ASN124 4.7 31.2 1.0
HE2 B:HIS125 4.7 32.9 1.0
HB3 B:ASP92 4.8 30.0 1.0
H B:HIS125 4.8 31.2 1.0
O B:LEU205 4.8 24.9 1.0
HE1 B:HIS66 4.8 36.4 1.0
NE2 B:HIS66 4.8 30.1 1.0
HE2 B:HIS248 4.9 31.8 1.0
H B:HIS248 4.9 31.6 1.0
N B:HIS248 4.9 26.2 1.0
NE2 B:HIS125 5.0 27.3 1.0
CG B:ASP64 5.0 27.3 1.0
NH1 B:ARG221 5.0 30.9 1.0
O B:HOH644 5.0 31.5 1.0

Manganese binding site 6 out of 12 in 6zee

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Manganese binding site 6 out of 12 in the Structure of PP1(7-300) Bound to PHACTR1 (507-580) at PH8.4


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 6 of Structure of PP1(7-300) Bound to PHACTR1 (507-580) at PH8.4 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mn502

b:37.8
occ:1.00
O B:HOH632 1.9 27.4 1.0
NE2 B:HIS66 2.0 30.1 1.0
OD1 B:ASP92 2.1 25.9 1.0
OD2 B:ASP64 2.2 26.8 1.0
O2 B:SO4516 2.2 31.4 1.0
O B:HOH644 2.3 31.5 1.0
CE1 B:HIS66 2.9 30.2 1.0
HE1 B:HIS66 3.0 36.4 1.0
CD2 B:HIS66 3.1 31.0 1.0
MN B:MN501 3.1 36.2 1.0
CG B:ASP92 3.2 26.8 1.0
S B:SO4516 3.3 32.6 1.0
HB3 B:ASP92 3.3 30.0 1.0
HD2 B:HIS66 3.3 37.3 1.0
O1 B:SO4516 3.4 28.4 1.0
CG B:ASP64 3.4 27.3 1.0
HH12 B:ARG96 3.5 39.8 0.5
CB B:ASP92 3.7 24.9 1.0
O4 B:SO4516 3.8 31.8 1.0
HB2 B:ASP92 3.8 30.0 1.0
HB3 B:ASP64 4.0 33.1 1.0
HE1 B:HIS173 4.0 31.0 1.0
HA B:HIS248 4.0 32.5 1.0
O B:HOH670 4.0 37.6 1.0
HE2 B:PHE267 4.0 33.5 1.0
HD2 B:HIS125 4.0 32.8 1.0
ND1 B:HIS66 4.1 29.9 1.0
NH1 B:ARG96 4.1 33.0 0.5
HH11 B:ARG96 4.1 39.8 0.5
CG B:HIS66 4.2 30.2 1.0
OD1 B:ASP64 4.3 26.3 1.0
OD2 B:ASP92 4.3 23.5 1.0
CB B:ASP64 4.3 27.5 1.0
OH B:TYR272 4.3 34.3 1.0
O B:HIS248 4.4 29.6 1.0
CD2 B:HIS125 4.4 27.2 1.0
HE B:ARG96 4.5 41.0 0.5
HH B:TYR272 4.5 41.3 1.0
NE2 B:HIS173 4.5 25.9 1.0
O3 B:SO4516 4.5 31.4 1.0
HE2 B:HIS125 4.5 32.9 1.0
CE1 B:HIS173 4.6 25.7 1.0
NE2 B:HIS125 4.7 27.3 1.0
HB2 B:ASP64 4.7 33.1 1.0
OD1 B:ASN124 4.8 26.1 1.0
CE2 B:PHE267 4.8 27.8 1.0
HD1 B:HIS66 4.8 36.1 1.0
CA B:HIS248 4.8 26.9 1.0
ND1 B:HIS248 4.8 26.9 1.0
C B:HIS248 4.9 28.3 1.0
HZ B:PHE267 4.9 34.5 1.0

Manganese binding site 7 out of 12 in 6zee

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Manganese binding site 7 out of 12 in the Structure of PP1(7-300) Bound to PHACTR1 (507-580) at PH8.4


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 7 of Structure of PP1(7-300) Bound to PHACTR1 (507-580) at PH8.4 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn501

b:33.6
occ:1.00
O A:HOH604 1.9 32.0 1.0
O4 A:SO4518 2.1 32.6 1.0
NE2 A:HIS173 2.2 26.9 1.0
OD1 A:ASN124 2.2 27.1 1.0
OD2 A:ASP92 2.2 27.1 1.0
ND1 A:HIS248 2.3 28.5 1.0
HE1 A:HIS248 2.8 34.2 1.0
CE1 A:HIS248 2.9 28.4 1.0
HA A:HIS248 3.0 34.7 1.0
HD21 A:ASN124 3.1 31.8 1.0
CD2 A:HIS173 3.1 26.0 1.0
MN A:MN502 3.2 37.4 1.0
CG A:ASP92 3.2 26.8 1.0
CE1 A:HIS173 3.2 26.8 1.0
CG A:ASN124 3.2 26.2 1.0
HD2 A:HIS173 3.3 31.4 1.0
HE1 A:HIS173 3.4 32.3 1.0
HD2 A:HIS125 3.4 33.6 1.0
S A:SO4518 3.4 35.8 1.0
ND2 A:ASN124 3.5 26.3 1.0
OD1 A:ASP92 3.5 26.2 1.0
CG A:HIS248 3.5 27.9 1.0
O3 A:SO4518 3.8 32.7 1.0
H A:ASN124 3.9 31.1 1.0
CA A:HIS248 3.9 28.8 1.0
OD2 A:ASP64 4.0 29.4 1.0
O2 A:SO4518 4.1 34.9 1.0
CB A:HIS248 4.1 27.4 1.0
O A:HIS248 4.1 32.2 1.0
NE2 A:HIS248 4.2 27.2 1.0
CD2 A:HIS125 4.2 27.9 1.0
ND1 A:HIS173 4.3 26.0 1.0
HB2 A:HIS248 4.3 33.1 1.0
CG A:HIS173 4.3 25.6 1.0
HD22 A:ASN124 4.4 31.8 1.0
O1 A:SO4518 4.4 33.4 1.0
CB A:ASP92 4.5 25.1 1.0
CD2 A:HIS248 4.5 27.7 1.0
HH12 A:ARG221 4.5 36.5 1.0
HB2 A:ASP92 4.5 30.2 1.0
C A:HIS248 4.5 30.5 1.0
CB A:ASN124 4.6 26.0 1.0
N A:ASN124 4.6 25.8 1.0
HE2 A:HIS125 4.6 36.1 1.0
H A:HIS125 4.7 29.4 1.0
O A:LEU205 4.7 24.6 1.0
HB3 A:ASP92 4.8 30.2 1.0
HB3 A:ASN124 4.8 31.3 1.0
H A:HIS248 4.8 31.9 1.0
HE2 A:HIS248 4.8 32.8 1.0
NE2 A:HIS125 4.8 29.9 1.0
N A:HIS248 4.9 26.5 1.0
NH1 A:ARG221 4.9 30.3 1.0
HH22 A:ARG221 4.9 36.7 1.0
HE1 A:HIS66 5.0 35.2 1.0
NE2 A:HIS66 5.0 30.0 1.0

Manganese binding site 8 out of 12 in 6zee

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Manganese binding site 8 out of 12 in the Structure of PP1(7-300) Bound to PHACTR1 (507-580) at PH8.4


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 8 of Structure of PP1(7-300) Bound to PHACTR1 (507-580) at PH8.4 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn502

b:37.4
occ:1.00
OD2 A:ASP64 2.1 29.4 1.0
NE2 A:HIS66 2.1 30.0 1.0
O A:HOH604 2.2 32.0 1.0
OD2 A:ASP92 2.2 27.1 1.0
O3 A:SO4518 2.3 32.7 1.0
O A:HOH606 2.4 32.4 1.0
CE1 A:HIS66 3.1 29.2 1.0
HO1 A:EDO508 3.1 50.2 1.0
CD2 A:HIS66 3.2 28.7 1.0
MN A:MN501 3.2 33.6 1.0
O4 A:SO4518 3.2 32.6 1.0
HE1 A:HIS66 3.2 35.2 1.0
CG A:ASP92 3.3 26.8 1.0
S A:SO4518 3.3 35.8 1.0
HB3 A:ASP92 3.3 30.2 1.0
HD2 A:HIS66 3.3 34.5 1.0
CG A:ASP64 3.4 28.6 1.0
CB A:ASP92 3.7 25.1 1.0
HB2 A:ASP92 3.8 30.2 1.0
HB3 A:ASP64 3.8 35.4 1.0
HE1 A:HIS173 3.8 32.3 1.0
HE1 A:PHE267 3.9 37.1 1.0
O2 A:SO4518 3.9 34.9 1.0
HA A:HIS248 3.9 34.7 1.0
HD2 A:HIS125 4.0 33.6 1.0
O1 A:EDO508 4.1 41.7 1.0
CB A:ASP64 4.2 29.4 1.0
ND1 A:HIS66 4.2 30.2 1.0
CG A:HIS66 4.3 28.4 1.0
OD1 A:ASP64 4.3 27.2 1.0
NE2 A:HIS173 4.3 26.9 1.0
HE A:ARG96 4.3 48.7 1.0
OD1 A:ASP92 4.4 26.2 1.0
H12 A:EDO508 4.4 44.2 1.0
CE1 A:HIS173 4.4 26.8 1.0
CD2 A:HIS125 4.4 27.9 1.0
O A:HIS248 4.4 32.2 1.0
OH A:TYR272 4.5 34.7 1.0
HE2 A:HIS125 4.5 36.1 1.0
O1 A:SO4518 4.5 33.4 1.0
H11 A:EDO508 4.5 44.2 1.0
C1 A:EDO508 4.6 36.7 1.0
HB2 A:ASP64 4.6 35.4 1.0
HH A:TYR272 4.6 41.8 1.0
NE2 A:HIS125 4.6 29.9 1.0
CE1 A:PHE267 4.7 30.8 1.0
CA A:HIS248 4.8 28.8 1.0
C A:HIS248 4.9 30.5 1.0
ND1 A:HIS248 4.9 28.5 1.0
H A:HIS248 5.0 31.9 1.0
OD1 A:ASN124 5.0 27.1 1.0
HD1 A:HIS66 5.0 36.4 1.0
HZ A:PHE267 5.0 38.9 1.0

Manganese binding site 9 out of 12 in 6zee

Go back to Manganese Binding Sites List in 6zee
Manganese binding site 9 out of 12 in the Structure of PP1(7-300) Bound to PHACTR1 (507-580) at PH8.4


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 9 of Structure of PP1(7-300) Bound to PHACTR1 (507-580) at PH8.4 within 5.0Å range:
probe atom residue distance (Å) B Occ
I:Mn501

b:34.5
occ:1.00
O4 I:SO4505 2.1 37.2 1.0
OD1 I:ASN124 2.1 39.7 1.0
ND1 I:HIS248 2.2 36.5 1.0
OD1 I:ASP92 2.2 40.5 1.0
NE2 I:HIS173 2.3 40.0 1.0
O I:HOH603 2.6 38.2 1.0
HE1 I:HIS248 2.7 43.2 1.0
CE1 I:HIS248 2.8 35.9 1.0
HA I:HIS248 2.9 45.0 1.0
CG I:ASP92 3.1 40.8 1.0
CG I:ASN124 3.1 39.0 1.0
HD21 I:ASN124 3.1 46.1 1.0
CE1 I:HIS173 3.2 40.4 1.0
MN I:MN502 3.2 45.2 1.0
S I:SO4505 3.3 42.0 1.0
CD2 I:HIS173 3.3 40.2 1.0
HE1 I:HIS173 3.4 47.7 1.0
OD2 I:ASP92 3.4 40.6 1.0
HD2 I:HIS173 3.5 47.4 1.0
CG I:HIS248 3.5 36.6 1.0
ND2 I:ASN124 3.5 38.7 1.0
HD2 I:HIS125 3.5 50.5 1.0
O3 I:SO4505 3.7 39.5 1.0
O2 I:SO4505 3.7 35.0 1.0
CA I:HIS248 3.8 37.4 1.0
H I:ASN124 3.9 47.0 1.0
OD2 I:ASP64 3.9 39.6 1.0
O I:HIS248 3.9 36.8 1.0
NE2 I:HIS248 4.1 35.6 1.0
CB I:HIS248 4.1 38.2 1.0
HB2 I:HIS248 4.3 46.0 1.0
HD22 I:ASN124 4.3 46.1 1.0
C I:HIS248 4.4 37.5 1.0
ND1 I:HIS173 4.4 40.9 1.0
CD2 I:HIS125 4.4 41.9 1.0
CD2 I:HIS248 4.4 36.9 1.0
CB I:ASP92 4.4 41.5 1.0
CG I:HIS173 4.4 40.8 1.0
O1 I:SO4505 4.5 33.4 1.0
CB I:ASN124 4.5 38.9 1.0
HB2 I:ASP92 4.5 49.0 1.0
HB3 I:ASN124 4.6 45.8 1.0
HH12 I:ARG221 4.6 46.1 1.0
N I:ASN124 4.6 39.8 1.0
HB3 I:ASP92 4.7 49.0 1.0
O I:LEU205 4.7 35.2 1.0
H I:HIS125 4.7 48.4 1.0
HE2 I:HIS248 4.8 42.9 1.0
H I:HIS248 4.8 44.7 1.0
CG I:ASP64 4.8 40.5 1.0
N I:HIS248 4.9 37.1 1.0
NE2 I:HIS66 4.9 44.1 1.0
HE2 I:HIS125 4.9 47.4 1.0
HB3 I:HIS248 5.0 46.0 1.0

Manganese binding site 10 out of 12 in 6zee

Go back to Manganese Binding Sites List in 6zee
Manganese binding site 10 out of 12 in the Structure of PP1(7-300) Bound to PHACTR1 (507-580) at PH8.4


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 10 of Structure of PP1(7-300) Bound to PHACTR1 (507-580) at PH8.4 within 5.0Å range:
probe atom residue distance (Å) B Occ
I:Mn502

b:45.2
occ:1.00
NE2 I:HIS66 1.9 44.1 1.0
O I:HOH603 2.0 38.2 1.0
O3 I:SO4505 2.1 39.5 1.0
OD1 I:ASP92 2.1 40.5 1.0
OD2 I:ASP64 2.3 39.6 1.0
CE1 I:HIS66 2.9 43.5 1.0
CD2 I:HIS66 3.0 42.4 1.0
S I:SO4505 3.1 42.0 1.0
HE1 I:HIS66 3.1 52.4 1.0
HD2 I:HIS66 3.2 51.0 1.0
CG I:ASP92 3.2 40.8 1.0
HB3 I:ASP92 3.2 49.0 1.0
O4 I:SO4505 3.2 37.2 1.0
MN I:MN501 3.2 34.5 1.0
HH12 I:ARG96 3.4 52.1 0.5
CG I:ASP64 3.5 40.5 1.0
O2 I:SO4505 3.6 35.0 1.0
CB I:ASP92 3.6 41.5 1.0
HD2 I:HIS125 3.8 50.5 1.0
HB3 I:ASP64 3.9 48.6 1.0
HB2 I:ASP92 3.9 49.0 1.0
HH11 I:ARG96 3.9 52.1 0.5
HE1 I:PHE267 3.9 46.5 1.0
NH1 I:ARG96 4.0 43.3 0.5
ND1 I:HIS66 4.0 43.5 1.0
CG I:HIS66 4.1 43.8 1.0
OH I:TYR272 4.1 45.1 1.0
HA I:HIS248 4.2 45.0 1.0
HE1 I:HIS173 4.2 47.7 1.0
CD2 I:HIS125 4.2 41.9 1.0
CB I:ASP64 4.3 41.2 1.0
OD2 I:ASP92 4.3 40.6 1.0
HH I:TYR272 4.3 54.3 1.0
O1 I:SO4505 4.3 33.4 1.0
O I:HIS248 4.3 36.8 1.0
HE2 I:HIS125 4.4 47.4 1.0
HE I:ARG96 4.4 53.3 0.5
OD1 I:ASP64 4.4 40.9 1.0
NE2 I:HIS125 4.6 39.4 1.0
NE2 I:HIS173 4.7 40.0 1.0
HB2 I:ASP64 4.7 48.6 1.0
CE1 I:PHE267 4.7 38.6 1.0
CE1 I:HIS173 4.7 40.4 1.0
HD1 I:HIS66 4.8 52.3 1.0
OD1 I:ASN124 4.8 39.7 1.0
HZ I:PHE267 4.8 46.9 1.0
ND1 I:HIS248 4.9 36.5 1.0
C I:HIS248 4.9 37.5 1.0
CZ I:TYR272 5.0 42.8 1.0
CA I:HIS248 5.0 37.4 1.0

Reference:

R.O.Fedoryshchak, M.Prechova, A.Butler, R.Lee, N.O'reilly, H.R.Flynn, A.P.Snijders, N.Eder, S.Ultanir, S.Mouilleron, R.Treisman. Molecular Basis For Substrate Specificity of the PHACTR1/PP1 Phosphatase Holoenzyme. Elife V. 9 2020.
ISSN: ESSN 2050-084X
PubMed: 32975518
DOI: 10.7554/ELIFE.61509
Page generated: Sun Oct 6 07:58:12 2024

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