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Manganese in PDB 1fjm: Protein Serine/Threonine Phosphatase-1 (Alpha Isoform, Type 1) Complexed with Microcystin-Lr Toxin

Enzymatic activity of Protein Serine/Threonine Phosphatase-1 (Alpha Isoform, Type 1) Complexed with Microcystin-Lr Toxin

All present enzymatic activity of Protein Serine/Threonine Phosphatase-1 (Alpha Isoform, Type 1) Complexed with Microcystin-Lr Toxin:
3.1.3.16;

Protein crystallography data

The structure of Protein Serine/Threonine Phosphatase-1 (Alpha Isoform, Type 1) Complexed with Microcystin-Lr Toxin, PDB code: 1fjm was solved by J.Goldberg, A.C.Nairn, J.Kuriyan, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 6.00 / 2.10
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 64.740, 77.110, 130.790, 90.00, 90.00, 90.00
R / Rfree (%) 17.8 / n/a

Manganese Binding Sites:

The binding sites of Manganese atom in the Protein Serine/Threonine Phosphatase-1 (Alpha Isoform, Type 1) Complexed with Microcystin-Lr Toxin (pdb code 1fjm). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 4 binding sites of Manganese where determined in the Protein Serine/Threonine Phosphatase-1 (Alpha Isoform, Type 1) Complexed with Microcystin-Lr Toxin, PDB code: 1fjm:
Jump to Manganese binding site number: 1; 2; 3; 4;

Manganese binding site 1 out of 4 in 1fjm

Go back to Manganese Binding Sites List in 1fjm
Manganese binding site 1 out of 4 in the Protein Serine/Threonine Phosphatase-1 (Alpha Isoform, Type 1) Complexed with Microcystin-Lr Toxin


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Protein Serine/Threonine Phosphatase-1 (Alpha Isoform, Type 1) Complexed with Microcystin-Lr Toxin within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn400

b:18.6
occ:1.00
 O A:HOH402 1.9 11.6 1.0
OD1 A:ASN124 2.0 17.1 1.0
NE2 A:HIS173 2.1 10.8 1.0
ND1 A:HIS248 2.3 20.6 1.0
OD2 A:ASP92 2.3 12.7 1.0
CG A:ASN124 3.0 13.8 1.0
CE1 A:HIS248 3.0 19.3 1.0
CE1 A:HIS173 3.1 9.7 1.0
CD2 A:HIS173 3.1 8.2 1.0
CG A:ASP92 3.2 10.8 1.0
MN A:MN401 3.3 21.1 1.0
O M:HOH9 3.3 17.4 1.0
OD1 A:ASP92 3.5 9.2 1.0
CG A:HIS248 3.5 19.8 1.0
ND2 A:ASN124 3.5 17.0 1.0
CA A:HIS248 3.7 19.0 1.0
CB A:HIS248 4.0 19.2 1.0
O A:HIS248 4.0 18.3 1.0
CD2 A:HIS125 4.0 13.3 1.0
OD2 A:ASP64 4.1 16.1 1.0
ND1 A:HIS173 4.3 12.1 1.0
NE2 A:HIS248 4.3 19.7 1.0
CB A:ASN124 4.3 13.1 1.0
CG A:HIS173 4.3 12.1 1.0
N A:ASN124 4.4 13.9 1.0
C A:HIS248 4.4 18.4 1.0
CB A:ASP92 4.4 12.2 1.0
CD2 A:HIS248 4.5 17.2 1.0
NE2 A:HIS125 4.6 14.3 1.0
N A:HIS248 4.6 19.4 1.0
O A:LEU205 4.7 16.9 1.0
CG A:ASP64 4.9 17.3 1.0
CA A:ASN124 4.9 13.8 1.0
O M:HOH8 4.9 18.6 1.0
OD1 A:ASP64 4.9 15.8 1.0

Manganese binding site 2 out of 4 in 1fjm

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Manganese binding site 2 out of 4 in the Protein Serine/Threonine Phosphatase-1 (Alpha Isoform, Type 1) Complexed with Microcystin-Lr Toxin


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of Protein Serine/Threonine Phosphatase-1 (Alpha Isoform, Type 1) Complexed with Microcystin-Lr Toxin within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn401

b:21.1
occ:1.00
 OD2 A:ASP64 2.0 16.1 1.0
O M:HOH8 2.1 18.6 1.0
O A:HOH402 2.2 11.6 1.0
OD2 A:ASP92 2.3 12.7 1.0
NE2 A:HIS66 2.3 13.3 1.0
CG A:ASP64 3.2 17.3 1.0
CE1 A:HIS66 3.2 15.1 1.0
MN A:MN400 3.3 18.6 1.0
CD2 A:HIS66 3.3 12.6 1.0
CG A:ASP92 3.3 10.8 1.0
CB A:ASP92 3.7 12.2 1.0
O M:HOH9 3.7 17.4 1.0
O A:HIS248 3.9 18.3 1.0
CB A:ASP64 4.0 14.9 1.0
OD1 A:ASP64 4.0 15.8 1.0
CE1 A:PHE267 4.2 16.1 1.0
CD2 A:HIS125 4.3 13.3 1.0
NE2 A:HIS125 4.3 14.3 1.0
O M:FGA6 4.3 29.2 1.0
ND1 A:HIS66 4.4 16.2 1.0
OD1 A:ASP92 4.4 9.2 1.0
CG A:HIS66 4.4 16.2 1.0
NE2 A:HIS173 4.5 10.8 1.0
C A:HIS248 4.6 18.4 1.0
CE1 A:HIS173 4.6 9.7 1.0
CA A:HIS248 4.6 19.0 1.0
OH A:TYR272 4.6 15.9 1.0
OD1 A:ASN124 4.7 17.1 1.0
ND1 A:HIS248 4.9 20.6 1.0
CZ A:PHE267 4.9 13.8 1.0
C M:FGA6 5.0 31.6 1.0

Manganese binding site 3 out of 4 in 1fjm

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Manganese binding site 3 out of 4 in the Protein Serine/Threonine Phosphatase-1 (Alpha Isoform, Type 1) Complexed with Microcystin-Lr Toxin


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 3 of Protein Serine/Threonine Phosphatase-1 (Alpha Isoform, Type 1) Complexed with Microcystin-Lr Toxin within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mn400

b:21.1
occ:1.00
 O B:HOH402 2.0 13.0 1.0
OD1 B:ASN124 2.0 18.3 1.0
NE2 B:HIS173 2.1 8.9 1.0
OD2 B:ASP92 2.2 14.5 1.0
ND1 B:HIS248 2.3 17.5 1.0
CE1 B:HIS173 3.0 9.0 1.0
CG B:ASN124 3.1 16.5 1.0
CE1 B:HIS248 3.1 16.1 1.0
CG B:ASP92 3.1 13.6 1.0
CD2 B:HIS173 3.1 8.0 1.0
MN B:MN401 3.2 18.9 1.0
OD1 B:ASP92 3.4 13.5 1.0
CG B:HIS248 3.4 18.6 1.0
O N:HOH131 3.6 13.2 1.0
ND2 B:ASN124 3.6 14.7 1.0
CA B:HIS248 3.6 16.7 1.0
CB B:HIS248 3.9 16.7 1.0
OD2 B:ASP64 4.0 12.3 1.0
O B:HIS248 4.1 23.0 1.0
CD2 B:HIS125 4.1 17.0 1.0
ND1 B:HIS173 4.2 9.9 1.0
CB B:ASN124 4.3 14.9 1.0
CG B:HIS173 4.3 10.5 1.0
N B:ASN124 4.3 13.5 1.0
NE2 B:HIS248 4.3 18.4 1.0
CB B:ASP92 4.4 12.7 1.0
C B:HIS248 4.4 21.0 1.0
CD2 B:HIS248 4.5 17.1 1.0
N B:HIS248 4.6 14.6 1.0
O B:LEU205 4.6 18.0 1.0
NE2 B:HIS125 4.7 19.1 1.0
CG B:ASP64 4.8 16.4 1.0
OD1 B:ASP64 4.8 13.5 1.0
CA B:ASN124 4.8 14.9 1.0

Manganese binding site 4 out of 4 in 1fjm

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Manganese binding site 4 out of 4 in the Protein Serine/Threonine Phosphatase-1 (Alpha Isoform, Type 1) Complexed with Microcystin-Lr Toxin


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 4 of Protein Serine/Threonine Phosphatase-1 (Alpha Isoform, Type 1) Complexed with Microcystin-Lr Toxin within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mn401

b:18.9
occ:1.00
 OD2 B:ASP64 1.9 12.3 1.0
O B:HOH402 2.1 13.0 1.0
OD2 B:ASP92 2.2 14.5 1.0
NE2 B:HIS66 2.3 18.6 1.0
O N:HOH128 2.3 19.2 1.0
CG B:ASP64 3.1 16.4 1.0
CE1 B:HIS66 3.2 18.7 1.0
MN B:MN400 3.2 21.1 1.0
CG B:ASP92 3.2 13.6 1.0
CD2 B:HIS66 3.4 17.5 1.0
CB B:ASP92 3.7 12.7 1.0
CB B:ASP64 3.9 13.4 1.0
O N:HOH131 4.0 13.2 1.0
OD1 B:ASP64 4.0 13.5 1.0
O B:HIS248 4.0 23.0 1.0
CE1 B:PHE267 4.3 18.2 1.0
CD2 B:HIS125 4.3 17.0 1.0
O N:FGA6 4.3 31.7 1.0
OD1 B:ASP92 4.3 13.5 1.0
NE2 B:HIS125 4.3 19.1 1.0
ND1 B:HIS66 4.4 14.9 1.0
CG B:HIS66 4.5 16.9 1.0
NE2 B:HIS173 4.5 8.9 1.0
CA B:HIS248 4.5 16.7 1.0
CE1 B:HIS173 4.6 9.0 1.0
C B:HIS248 4.6 21.0 1.0
OH B:TYR272 4.6 18.8 1.0
OD1 B:ASN124 4.6 18.3 1.0
ND1 B:HIS248 4.9 17.5 1.0
CZ B:PHE267 4.9 19.1 1.0
C N:FGA6 5.0 30.4 1.0

Reference:

J.Goldberg, H.B.Huang, Y.G.Kwon, P.Greengard, A.C.Nairn, J.Kuriyan. Three-Dimensional Structure of the Catalytic Subunit of Protein Serine/Threonine Phosphatase-1. Nature V. 376 745 1995.
ISSN: ISSN 0028-0836
PubMed: 7651533
DOI: 10.1038/376745A0
Page generated: Sat Oct 5 10:23:58 2024

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