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Manganese in PDB 6alz: Crystal Structure of Protein Phosphatase 1 Bound to the Natural Inhibitor Tautomycetin

Enzymatic activity of Crystal Structure of Protein Phosphatase 1 Bound to the Natural Inhibitor Tautomycetin

All present enzymatic activity of Crystal Structure of Protein Phosphatase 1 Bound to the Natural Inhibitor Tautomycetin:
3.1.3.16;

Protein crystallography data

The structure of Crystal Structure of Protein Phosphatase 1 Bound to the Natural Inhibitor Tautomycetin, PDB code: 6alz was solved by M.S.Choy, W.Peti, R.Page, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 38.82 / 2.21
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 66.199, 78.855, 133.779, 90.00, 90.00, 90.00
R / Rfree (%) 18.4 / 21.6

Other elements in 6alz:

The structure of Crystal Structure of Protein Phosphatase 1 Bound to the Natural Inhibitor Tautomycetin also contains other interesting chemical elements:

Chlorine (Cl) 4 atoms

Manganese Binding Sites:

The binding sites of Manganese atom in the Crystal Structure of Protein Phosphatase 1 Bound to the Natural Inhibitor Tautomycetin (pdb code 6alz). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 4 binding sites of Manganese where determined in the Crystal Structure of Protein Phosphatase 1 Bound to the Natural Inhibitor Tautomycetin, PDB code: 6alz:
Jump to Manganese binding site number: 1; 2; 3; 4;

Manganese binding site 1 out of 4 in 6alz

Go back to Manganese Binding Sites List in 6alz
Manganese binding site 1 out of 4 in the Crystal Structure of Protein Phosphatase 1 Bound to the Natural Inhibitor Tautomycetin


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Crystal Structure of Protein Phosphatase 1 Bound to the Natural Inhibitor Tautomycetin within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn401

b:30.1
occ:1.00
 O A:HOH543 2.0 30.1 1.0
OD1 A:ASN124 2.1 33.0 1.0
NE2 A:HIS173 2.2 29.7 1.0
OD2 A:ASP92 2.3 30.6 1.0
ND1 A:HIS248 2.3 34.5 1.0
CE1 A:HIS248 3.0 35.4 1.0
CE1 A:HIS173 3.1 29.0 1.0
CG A:ASN124 3.1 30.0 1.0
CG A:ASP92 3.1 31.3 1.0
CD2 A:HIS173 3.2 28.8 1.0
MN A:MN402 3.3 29.9 1.0
OD1 A:ASP92 3.4 25.4 1.0
CG A:HIS248 3.5 33.1 1.0
CA A:HIS248 3.7 33.0 1.0
ND2 A:ASN124 3.7 34.6 1.0
O A:HOH547 3.8 32.5 1.0
OD2 A:ASP64 4.0 32.0 1.0
O A:HIS248 4.0 33.5 1.0
CB A:HIS248 4.0 31.5 1.0
CD2 A:HIS125 4.2 28.5 1.0
ND1 A:HIS173 4.2 24.5 1.0
NE2 A:HIS248 4.3 34.4 1.0
CB A:ASN124 4.3 30.4 1.0
C A:HIS248 4.3 35.0 1.0
CG A:HIS173 4.3 30.2 1.0
N A:ASN124 4.4 28.0 1.0
CB A:ASP92 4.5 30.6 1.0
CD2 A:HIS248 4.5 32.9 1.0
N A:HIS248 4.6 32.2 1.0
O A:LEU205 4.7 33.7 1.0
CG A:ASP64 4.8 29.6 1.0
OD1 A:ASP64 4.8 30.9 1.0
O A:HOH504 4.9 31.2 1.0
NE2 A:HIS125 4.9 30.0 1.0
O37 A:BKM403 4.9 41.2 1.0
CA A:ASN124 4.9 32.1 1.0

Manganese binding site 2 out of 4 in 6alz

Go back to Manganese Binding Sites List in 6alz
Manganese binding site 2 out of 4 in the Crystal Structure of Protein Phosphatase 1 Bound to the Natural Inhibitor Tautomycetin


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of Crystal Structure of Protein Phosphatase 1 Bound to the Natural Inhibitor Tautomycetin within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn402

b:29.9
occ:1.00
 OD2 A:ASP64 1.9 32.0 1.0
OD2 A:ASP92 2.1 30.6 1.0
NE2 A:HIS66 2.1 29.2 1.0
O A:HOH543 2.2 30.1 1.0
O A:HOH504 2.2 31.2 1.0
CE1 A:HIS66 3.0 29.8 1.0
CG A:ASP64 3.1 29.6 1.0
CD2 A:HIS66 3.2 30.9 1.0
CG A:ASP92 3.2 31.3 1.0
MN A:MN401 3.3 30.1 1.0
CB A:ASP92 3.7 30.6 1.0
O37 A:BKM403 3.8 41.2 1.0
CB A:ASP64 3.9 26.0 1.0
O A:HOH547 3.9 32.5 1.0
OD1 A:ASP64 4.0 30.9 1.0
O A:HIS248 4.1 33.5 1.0
CD2 A:HIS125 4.1 28.5 1.0
ND1 A:HIS66 4.2 24.9 1.0
OD1 A:ASP92 4.3 25.4 1.0
CG A:HIS66 4.3 30.5 1.0
OH A:TYR272 4.4 34.8 1.0
NE2 A:HIS125 4.4 30.0 1.0
CE2 A:PHE267 4.4 30.3 1.0
NE2 A:HIS173 4.7 29.7 1.0
C A:HIS248 4.7 35.0 1.0
CE1 A:HIS173 4.7 29.0 1.0
OD1 A:ASN124 4.7 33.0 1.0
CA A:HIS248 4.7 33.0 1.0
C35 A:BKM403 4.9 36.9 1.0

Manganese binding site 3 out of 4 in 6alz

Go back to Manganese Binding Sites List in 6alz
Manganese binding site 3 out of 4 in the Crystal Structure of Protein Phosphatase 1 Bound to the Natural Inhibitor Tautomycetin


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 3 of Crystal Structure of Protein Phosphatase 1 Bound to the Natural Inhibitor Tautomycetin within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mn401

b:35.2
occ:1.00
 OD2 B:ASP92 2.1 34.2 1.0
O B:HOH510 2.1 31.6 1.0
OD2 B:ASP64 2.1 34.2 1.0
NE2 B:HIS66 2.1 32.7 1.0
O B:HOH546 2.2 33.6 1.0
CE1 B:HIS66 3.1 30.5 1.0
CG B:ASP92 3.2 34.4 1.0
CD2 B:HIS66 3.2 35.0 1.0
CG B:ASP64 3.2 33.3 1.0
MN B:MN402 3.3 34.8 1.0
CB B:ASP92 3.7 33.3 1.0
O37 B:BKM403 3.9 46.8 1.0
O B:HOH516 4.0 42.1 1.0
CB B:ASP64 4.0 30.9 1.0
OD1 B:ASP64 4.1 33.4 1.0
O B:HIS248 4.1 38.7 1.0
ND1 B:HIS66 4.2 29.8 1.0
OD1 B:ASP92 4.2 30.4 1.0
CD2 B:HIS125 4.2 37.3 1.0
CG B:HIS66 4.3 31.6 1.0
NE2 B:HIS125 4.4 38.0 1.0
OH B:TYR272 4.4 40.1 1.0
CE2 B:PHE267 4.5 36.5 1.0
C B:HIS248 4.7 35.8 1.0
CA B:HIS248 4.7 37.3 1.0
OD1 B:ASN124 4.7 40.8 1.0
NE2 B:HIS173 4.7 37.5 1.0
CE1 B:HIS173 4.7 34.5 1.0
C35 B:BKM403 4.8 44.4 1.0
ND1 B:HIS248 4.9 42.9 1.0

Manganese binding site 4 out of 4 in 6alz

Go back to Manganese Binding Sites List in 6alz
Manganese binding site 4 out of 4 in the Crystal Structure of Protein Phosphatase 1 Bound to the Natural Inhibitor Tautomycetin


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 4 of Crystal Structure of Protein Phosphatase 1 Bound to the Natural Inhibitor Tautomycetin within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mn402

b:34.8
occ:1.00
 O B:HOH510 1.9 31.6 1.0
OD1 B:ASN124 2.1 40.8 1.0
NE2 B:HIS173 2.2 37.5 1.0
OD2 B:ASP92 2.3 34.2 1.0
ND1 B:HIS248 2.3 42.9 1.0
CE1 B:HIS248 3.0 46.5 1.0
CG B:ASP92 3.0 34.4 1.0
CE1 B:HIS173 3.1 34.5 1.0
CG B:ASN124 3.1 38.6 1.0
CD2 B:HIS173 3.2 36.5 1.0
OD1 B:ASP92 3.2 30.4 1.0
MN B:MN401 3.3 35.2 1.0
CG B:HIS248 3.5 41.5 1.0
CA B:HIS248 3.6 37.3 1.0
ND2 B:ASN124 3.7 38.2 1.0
OD2 B:ASP64 3.9 34.2 1.0
CB B:HIS248 4.0 38.8 1.0
O B:HOH516 4.0 42.1 1.0
O B:HIS248 4.1 38.7 1.0
NE2 B:HIS248 4.2 40.2 1.0
ND1 B:HIS173 4.2 32.1 1.0
CD2 B:HIS125 4.2 37.3 1.0
CG B:HIS173 4.3 36.6 1.0
CB B:ASN124 4.3 36.9 1.0
CB B:ASP92 4.4 33.3 1.0
C B:HIS248 4.4 35.8 1.0
N B:ASN124 4.4 38.0 1.0
CD2 B:HIS248 4.4 39.6 1.0
N B:HIS248 4.5 35.6 1.0
CG B:ASP64 4.7 33.3 1.0
OD1 B:ASP64 4.8 33.4 1.0
O B:LEU205 4.8 41.2 1.0
O37 B:BKM403 4.9 46.8 1.0
NE2 B:HIS125 4.9 38.0 1.0
CA B:ASN124 4.9 38.2 1.0
O B:HOH546 5.0 33.6 1.0

Reference:

M.S.Choy, M.Swingle, B.D'arcy, K.Abney, S.F.Rusin, A.N.Kettenbach, R.Page, R.E.Honkanen, W.Peti. PP1:Tautomycetin Complex Reveals A Path Toward the Development of PP1-Specific Inhibitors. J. Am. Chem. Soc. V. 139 17703 2017.
ISSN: ESSN 1520-5126
PubMed: 29156132
DOI: 10.1021/JACS.7B09368
Page generated: Sun Oct 6 03:51:25 2024

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