Atomistry » Manganese » PDB 1en6-1g0i » 1fjm
Atomistry »
  Manganese »
    PDB 1en6-1g0i »
      1fjm »

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

Go back to Manganese Binding Sites List in 1fjm
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

Go back to Manganese Binding Sites List in 1fjm
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

Go back to Manganese Binding Sites List in 1fjm
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

Last articles

Zn in 9JPJ
Zn in 9JP7
Zn in 9JPK
Zn in 9JPL
Zn in 9GN6
Zn in 9GN7
Zn in 9GKU
Zn in 9GKW
Zn in 9GKX
Zn in 9GL0
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy