Manganese in PDB 6zeg: Structure of PP1-IRSP53 Chimera [PP1(7-304) + Linker (G/S)X9 + IRSP53(449-465)] Bound to PHACTR1 (516-580)

Enzymatic activity of Structure of PP1-IRSP53 Chimera [PP1(7-304) + Linker (G/S)X9 + IRSP53(449-465)] Bound to PHACTR1 (516-580)

All present enzymatic activity of Structure of PP1-IRSP53 Chimera [PP1(7-304) + Linker (G/S)X9 + IRSP53(449-465)] Bound to PHACTR1 (516-580):
3.1.3.16;

Protein crystallography data

The structure of Structure of PP1-IRSP53 Chimera [PP1(7-304) + Linker (G/S)X9 + IRSP53(449-465)] Bound to PHACTR1 (516-580), PDB code: 6zeg 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) 37.18 / 1.09
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 48.616, 122.394, 69.097, 90.00, 92.22, 90.00
R / Rfree (%) 12 / 14

Manganese Binding Sites:

The binding sites of Manganese atom in the Structure of PP1-IRSP53 Chimera [PP1(7-304) + Linker (G/S)X9 + IRSP53(449-465)] Bound to PHACTR1 (516-580) (pdb code 6zeg). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 4 binding sites of Manganese where determined in the Structure of PP1-IRSP53 Chimera [PP1(7-304) + Linker (G/S)X9 + IRSP53(449-465)] Bound to PHACTR1 (516-580), PDB code: 6zeg:
Jump to Manganese binding site number: 1; 2; 3; 4;

Manganese binding site 1 out of 4 in 6zeg

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Manganese binding site 1 out of 4 in the Structure of PP1-IRSP53 Chimera [PP1(7-304) + Linker (G/S)X9 + IRSP53(449-465)] Bound to PHACTR1 (516-580)


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-IRSP53 Chimera [PP1(7-304) + Linker (G/S)X9 + IRSP53(449-465)] Bound to PHACTR1 (516-580) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn501

b:6.4
occ:1.00
 OD1 A:ASN124 2.1 7.0 1.0
ND1 A:HIS248 2.2 6.9 1.0
NE2 A:HIS173 2.2 6.5 1.0
OD2 A:ASP92 2.2 6.3 1.0
O4 A:PO4503 2.3 8.1 1.0
O3 A:PO4503 2.3 8.1 1.0
P A:PO4503 2.9 7.5 1.0
CE1 A:HIS248 3.1 6.9 1.0
HA A:HIS248 3.1 8.0 1.0
HE1 A:HIS248 3.1 8.3 1.0
CG A:ASP92 3.1 6.3 1.0
CG A:ASN124 3.2 7.1 1.0
CD2 A:HIS173 3.2 6.8 1.0
HD21 A:ASN124 3.2 9.6 1.0
CE1 A:HIS173 3.2 6.5 1.0
HD2 A:HIS125 3.3 9.3 1.0
HD2 A:HIS173 3.3 8.2 1.0
CG A:HIS248 3.3 6.6 1.0
HE1 A:HIS173 3.4 7.8 1.0
MN A:MN502 3.4 6.9 1.0
OD1 A:ASP92 3.4 6.7 1.0
ND2 A:ASN124 3.6 8.0 1.0
HB2 A:HIS248 3.8 8.3 1.0
H A:ASN124 3.8 7.9 1.0
CB A:HIS248 3.8 6.9 1.0
CA A:HIS248 3.9 6.6 1.0
O1 A:PO4503 3.9 9.9 1.0
O2 A:PO4503 4.0 7.5 1.0
CD2 A:HIS125 4.1 7.7 1.0
OD2 A:ASP64 4.1 8.0 1.0
NE2 A:HIS248 4.3 7.5 1.0
HE2 A:HIS125 4.3 9.8 1.0
O A:HIS248 4.3 8.4 1.0
ND1 A:HIS173 4.3 6.7 1.0
CG A:HIS173 4.4 6.7 1.0
CD2 A:HIS248 4.4 6.9 1.0
HD22 A:ASN124 4.4 9.6 1.0
CB A:ASP92 4.5 6.3 1.0
CB A:ASN124 4.5 7.2 1.0
HB2 A:ASP92 4.5 7.6 1.0
N A:ASN124 4.6 6.6 1.0
H A:HIS125 4.6 8.1 1.0
NE2 A:HIS125 4.6 8.2 1.0
HH12 A:ARG221 4.6 10.0 1.0
C A:HIS248 4.6 7.0 1.0
HB3 A:ASN124 4.6 8.6 1.0
O A:LEU205 4.7 8.0 1.0
HB3 A:ASP92 4.8 7.6 1.0
HB3 A:HIS248 4.8 8.3 1.0
H A:HIS248 4.8 7.7 1.0
N A:HIS248 4.9 6.4 1.0
HE2 A:HIS248 5.0 9.0 1.0
HH22 A:ARG221 5.0 10.0 1.0

Manganese binding site 2 out of 4 in 6zeg

Go back to Manganese Binding Sites List in 6zeg
Manganese binding site 2 out of 4 in the Structure of PP1-IRSP53 Chimera [PP1(7-304) + Linker (G/S)X9 + IRSP53(449-465)] Bound to PHACTR1 (516-580)


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-IRSP53 Chimera [PP1(7-304) + Linker (G/S)X9 + IRSP53(449-465)] Bound to PHACTR1 (516-580) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn502

b:6.9
occ:1.00
 O4 A:PO4503 2.0 8.1 1.0
OD2 A:ASP64 2.1 8.0 1.0
NE2 A:HIS66 2.2 7.8 1.0
OD2 A:ASP92 2.2 6.3 1.0
O A:HOH831 2.2 8.8 1.0
O1 A:PO4503 2.9 9.9 1.0
P A:PO4503 3.1 7.5 1.0
CD2 A:HIS66 3.1 7.6 1.0
CE1 A:HIS66 3.2 7.7 1.0
HB3 A:ASP92 3.2 7.6 1.0
CG A:ASP64 3.2 7.4 1.0
HD2 A:HIS66 3.3 9.1 1.0
CG A:ASP92 3.3 6.3 1.0
HE1 A:HIS66 3.4 9.3 1.0
MN A:MN501 3.4 6.4 1.0
HB3 A:ASP64 3.5 8.6 1.0
HE1 A:PHE267 3.6 10.9 1.0
CB A:ASP92 3.6 6.3 1.0
HA A:HIS248 3.7 8.0 1.0
HB2 A:ASP92 3.7 7.6 1.0
CB A:ASP64 3.9 7.2 1.0
HE1 A:HIS173 3.9 7.8 1.0
O3 A:PO4503 3.9 8.1 1.0
HD2 A:HIS125 4.0 9.3 1.0
O A:HOH623 4.1 10.8 1.0
O A:HOH631 4.1 10.9 1.0
O2 A:PO4503 4.1 7.5 1.0
HE2 A:HIS125 4.2 9.8 1.0
OD1 A:ASP64 4.2 7.7 1.0
HB2 A:ASP64 4.2 8.6 1.0
ND1 A:HIS66 4.3 7.7 1.0
CG A:HIS66 4.3 7.2 1.0
CD2 A:HIS125 4.4 7.7 1.0
OD1 A:ASP92 4.4 6.7 1.0
CE1 A:PHE267 4.4 9.1 1.0
NE2 A:HIS125 4.5 8.2 1.0
NE2 A:HIS173 4.5 6.5 1.0
CE1 A:HIS173 4.5 6.5 1.0
CA A:HIS248 4.6 6.6 1.0
O A:HIS248 4.7 8.4 1.0
HH A:TYR272 4.7 15.1 1.0
H A:HIS248 4.8 7.7 1.0
OH A:TYR272 4.8 12.6 1.0
C A:HIS248 4.9 7.0 1.0
HZ A:PHE267 4.9 12.2 1.0
ND1 A:HIS248 5.0 6.9 1.0

Manganese binding site 3 out of 4 in 6zeg

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Manganese binding site 3 out of 4 in the Structure of PP1-IRSP53 Chimera [PP1(7-304) + Linker (G/S)X9 + IRSP53(449-465)] Bound to PHACTR1 (516-580)


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-IRSP53 Chimera [PP1(7-304) + Linker (G/S)X9 + IRSP53(449-465)] Bound to PHACTR1 (516-580) within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mn501

b:7.4
occ:1.00
 OD1 B:ASN124 2.1 7.8 1.0
ND1 B:HIS248 2.2 7.7 1.0
NE2 B:HIS173 2.2 7.0 1.0
OD2 B:ASP92 2.3 7.7 1.0
O1 B:PO4503 2.3 9.6 1.0
O3 B:PO4503 2.3 8.7 1.0
P B:PO4503 2.9 8.7 1.0
HA B:HIS248 3.1 9.3 1.0
CE1 B:HIS248 3.1 7.9 1.0
CG B:ASN124 3.1 8.0 1.0
HE1 B:HIS248 3.2 9.5 1.0
CG B:ASP92 3.2 7.3 1.0
CD2 B:HIS173 3.2 7.0 1.0
HD21 B:ASN124 3.2 10.6 1.0
HD2 B:HIS125 3.2 9.6 1.0
CE1 B:HIS173 3.2 7.3 1.0
CG B:HIS248 3.3 7.7 1.0
HD2 B:HIS173 3.3 8.4 1.0
HE1 B:HIS173 3.4 8.8 1.0
MN B:MN502 3.4 8.1 1.0
OD1 B:ASP92 3.4 7.5 1.0
ND2 B:ASN124 3.6 8.8 1.0
HB2 B:HIS248 3.7 8.9 1.0
CB B:HIS248 3.8 7.4 1.0
H B:ASN124 3.8 8.8 1.0
CA B:HIS248 3.9 7.8 1.0
O2 B:PO4503 3.9 10.1 1.0
O4 B:PO4503 4.0 8.9 1.0
CD2 B:HIS125 4.0 8.0 1.0
OD2 B:ASP64 4.2 8.4 1.0
HE2 B:HIS125 4.2 10.7 1.0
NE2 B:HIS248 4.3 8.2 1.0
O B:HIS248 4.3 9.6 1.0
ND1 B:HIS173 4.3 7.0 1.0
CG B:HIS173 4.4 7.1 1.0
CD2 B:HIS248 4.4 7.9 1.0
HD22 B:ASN124 4.4 10.6 1.0
CB B:ASN124 4.5 8.5 1.0
CB B:ASP92 4.5 7.9 1.0
NE2 B:HIS125 4.5 8.9 1.0
HB2 B:ASP92 4.5 9.5 1.0
N B:ASN124 4.6 7.4 1.0
HH12 B:ARG221 4.6 11.5 1.0
H B:HIS125 4.6 9.2 1.0
C B:HIS248 4.6 8.6 1.0
HB3 B:ASN124 4.6 10.2 1.0
O B:LEU205 4.7 8.6 1.0
HB3 B:HIS248 4.8 8.9 1.0
HB3 B:ASP92 4.8 9.5 1.0
H B:HIS248 4.8 9.1 1.0
N B:HIS248 4.9 7.6 1.0
HH22 B:ARG221 5.0 11.3 1.0

Manganese binding site 4 out of 4 in 6zeg

Go back to Manganese Binding Sites List in 6zeg
Manganese binding site 4 out of 4 in the Structure of PP1-IRSP53 Chimera [PP1(7-304) + Linker (G/S)X9 + IRSP53(449-465)] Bound to PHACTR1 (516-580)


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-IRSP53 Chimera [PP1(7-304) + Linker (G/S)X9 + IRSP53(449-465)] Bound to PHACTR1 (516-580) within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mn502

b:8.1
occ:1.00
 OD2 B:ASP64 2.1 8.4 1.0
O1 B:PO4503 2.1 9.6 1.0
NE2 B:HIS66 2.2 8.6 1.0
OD2 B:ASP92 2.3 7.7 1.0
O B:HOH804 2.3 9.9 1.0
O2 B:PO4503 2.9 10.1 1.0
P B:PO4503 3.1 8.7 1.0
CE1 B:HIS66 3.1 8.6 1.0
CD2 B:HIS66 3.1 8.3 1.0
HB3 B:ASP92 3.2 9.5 1.0
CG B:ASP64 3.2 7.6 1.0
CG B:ASP92 3.3 7.3 1.0
HE1 B:HIS66 3.3 10.3 1.0
HD2 B:HIS66 3.3 9.9 1.0
MN B:MN501 3.4 7.4 1.0
HB3 B:ASP64 3.5 9.5 1.0
HE1 B:PHE267 3.6 12.9 1.0
CB B:ASP92 3.6 7.9 1.0
HA B:HIS248 3.7 9.3 1.0
HB2 B:ASP92 3.7 9.5 1.0
CB B:ASP64 3.9 7.9 1.0
HE1 B:HIS173 3.9 8.8 1.0
HD2 B:HIS125 3.9 9.6 1.0
O3 B:PO4503 3.9 8.7 1.0
O B:HOH631 4.0 11.9 1.0
O B:HOH653 4.1 11.7 1.0
OD1 B:ASP64 4.2 8.8 1.0
O4 B:PO4503 4.2 8.9 1.0
HE2 B:HIS125 4.2 10.7 1.0
HB2 B:ASP64 4.2 9.5 1.0
ND1 B:HIS66 4.3 9.1 1.0
CG B:HIS66 4.3 8.6 1.0
CD2 B:HIS125 4.3 8.0 1.0
OD1 B:ASP92 4.4 7.5 1.0
CE1 B:PHE267 4.5 10.7 1.0
NE2 B:HIS125 4.5 8.9 1.0
CE1 B:HIS173 4.5 7.3 1.0
NE2 B:HIS173 4.5 7.0 1.0
CA B:HIS248 4.6 7.8 1.0
H B:HIS248 4.7 9.1 1.0
O B:HIS248 4.8 9.6 1.0
HH B:TYR272 4.8 14.8 1.0
C B:HIS248 4.9 8.6 1.0
OH B:TYR272 4.9 12.3 1.0
HZ B:PHE267 4.9 14.0 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: Tue Dec 15 05:10:17 2020

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