Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0016311 | biological_process | dephosphorylation |
A | 0016791 | molecular_function | phosphatase activity |
B | 0016311 | biological_process | dephosphorylation |
B | 0016791 | molecular_function | phosphatase activity |
C | 0016311 | biological_process | dephosphorylation |
C | 0016791 | molecular_function | phosphatase activity |
D | 0016311 | biological_process | dephosphorylation |
D | 0016791 | molecular_function | phosphatase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 13 |
Details | binding site for residue TLA A 401 |
Chain | Residue |
A | ASP92 |
A | THR131 |
A | HOH544 |
A | HOH561 |
A | HOH574 |
A | HIS93 |
A | CYS124 |
A | LYS125 |
A | ALA126 |
A | GLY127 |
A | LYS128 |
A | GLY129 |
A | ARG130 |
site_id | AC2 |
Number of Residues | 11 |
Details | binding site for residue TLA B 401 |
Chain | Residue |
B | ASP92 |
B | CYS124 |
B | LYS125 |
B | ALA126 |
B | GLY127 |
B | LYS128 |
B | GLY129 |
B | ARG130 |
B | THR131 |
B | GLN171 |
B | HOH564 |
site_id | AC3 |
Number of Residues | 10 |
Details | binding site for residue TLA C 401 |
Chain | Residue |
C | ASP92 |
C | HIS93 |
C | LYS125 |
C | ALA126 |
C | GLY127 |
C | LYS128 |
C | GLY129 |
C | ARG130 |
C | THR131 |
C | GLN171 |
site_id | AC4 |
Number of Residues | 13 |
Details | binding site for residue TLA D 401 |
Chain | Residue |
D | ASP92 |
D | HIS93 |
D | CYS124 |
D | LYS125 |
D | ALA126 |
D | GLY127 |
D | LYS128 |
D | GLY129 |
D | ARG130 |
D | THR131 |
D | GLN171 |
D | HOH503 |
D | HOH513 |
Functional Information from PROSITE/UniProt
site_id | PS00383 |
Number of Residues | 11 |
Details | TYR_PHOSPHATASE_1 Tyrosine specific protein phosphatases active site. IHCkaGkgRTG |
Chain | Residue | Details |
A | ILE122-GLY132 | |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 684 |
Details | Domain: {"description":"Phosphatase tensin-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU00590","evidenceCode":"ECO:0000255"}]} |
site_id | SWS_FT_FI2 |
Number of Residues | 40 |
Details | Region: {"description":"Required for interaction with NOP53","evidences":[{"source":"PubMed","id":"15355975","evidenceCode":"ECO:0000269"}]} |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | Active site: {"description":"Phosphocysteine intermediate","evidences":[{"source":"PROSITE-ProRule","id":"PRU00590","evidenceCode":"ECO:0000255"}]} |
site_id | SWS_FT_FI4 |
Number of Residues | 8 |
Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"26166433","evidenceCode":"ECO:0000269"}]} |
site_id | SWS_FT_FI5 |
Number of Residues | 4 |
Details | Modified residue: {"description":"Phosphotyrosine; by FRK","evidences":[{"source":"PubMed","id":"19345329","evidenceCode":"ECO:0000269"}]} |
Catalytic Information from CSA
site_id | MCSA1 |
Number of Residues | 3 |
Details | M-CSA 456 |
Chain | Residue | Details |
A | ASP92 | proton shuttle (general acid/base) |
A | CYS124 | covalent catalysis |
A | ARG130 | transition state stabiliser |
site_id | MCSA2 |
Number of Residues | 3 |
Details | M-CSA 456 |
Chain | Residue | Details |
B | ASP92 | proton shuttle (general acid/base) |
B | CYS124 | covalent catalysis |
B | ARG130 | transition state stabiliser |
site_id | MCSA3 |
Number of Residues | 3 |
Details | M-CSA 456 |
Chain | Residue | Details |
C | ASP92 | proton shuttle (general acid/base) |
C | CYS124 | covalent catalysis |
C | ARG130 | transition state stabiliser |
site_id | MCSA4 |
Number of Residues | 3 |
Details | M-CSA 456 |
Chain | Residue | Details |
D | ASP92 | proton shuttle (general acid/base) |
D | CYS124 | covalent catalysis |
D | ARG130 | transition state stabiliser |