8U1E
Apo protein tyrosine phosphatase 1B (PTP1B) at high resolution (1.43 A) in space group P43212 with two distinctly ordered chains
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004725 | molecular_function | protein tyrosine phosphatase activity |
| A | 0006470 | biological_process | protein dephosphorylation |
| A | 0016311 | biological_process | dephosphorylation |
| B | 0004725 | molecular_function | protein tyrosine phosphatase activity |
| B | 0006470 | biological_process | protein dephosphorylation |
| B | 0016311 | biological_process | dephosphorylation |
Functional Information from PROSITE/UniProt
| site_id | PS00383 |
| Number of Residues | 11 |
| Details | TYR_PHOSPHATASE_1 Tyrosine specific protein phosphatases active site. VHCsaGigRSG |
| Chain | Residue | Details |
| A | VAL213-GLY223 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 548 |
| Details | Domain: {"description":"Tyrosine-protein phosphatase","evidences":[{"source":"PROSITE-ProRule","id":"PRU00160","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Phosphocysteine intermediate"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Binding site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 14 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N-acetylmethionine","evidences":[{"source":"PubMed","id":"2546149","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"15592455","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine; by PKB/AKT1, CLK1 and CLK2","evidences":[{"source":"PubMed","id":"10480872","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11579209","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphotyrosine; by EGFR","evidences":[{"source":"PubMed","id":"9355745","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"S-nitrosocysteine; in reversibly inhibited form","evidences":[{"source":"PubMed","id":"22169477","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"Phosphoserine; by CLK1 and CLK2","evidences":[{"source":"PubMed","id":"10480872","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI11 |
| Number of Residues | 4 |
| Details | Cross-link: {"description":"N,N-(cysteine-1,S-diyl)serine (Cys-Ser); in inhibited form","evidences":[{"source":"PubMed","id":"12802338","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12802339","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 5 |
| Details | M-CSA 469 |
| Chain | Residue | Details |
| A | ASP181 | proton shuttle (general acid/base) |
| A | CYS215 | covalent catalysis |
| A | ARG221 | activator, electrostatic stabiliser |
| A | SER222 | activator, electrostatic stabiliser |
| A | GLN262 | steric role |
| site_id | MCSA2 |
| Number of Residues | 5 |
| Details | M-CSA 469 |
| Chain | Residue | Details |
| B | ASP181 | proton shuttle (general acid/base) |
| B | CYS215 | covalent catalysis |
| B | ARG221 | activator, electrostatic stabiliser |
| B | SER222 | activator, electrostatic stabiliser |
| B | GLN262 | steric role |
