4Y14
Structure of protein tyrosine phosphatase 1B complexed with inhibitor (PTP1B:CPT157633)
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 PDB Data
| site_id | AC1 |
| Number of Residues | 2 |
| Details | binding site for residue CL A 401 |
| Chain | Residue |
| A | PRO38 |
| A | LYS39 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | binding site for residue CL A 402 |
| Chain | Residue |
| A | ARG24 |
| A | ARG254 |
| A | GLN262 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | binding site for residue CL A 403 |
| Chain | Residue |
| A | ARG112 |
| A | VAL113 |
| A | HIS175 |
| site_id | AC4 |
| Number of Residues | 8 |
| Details | binding site for residue TRS A 404 |
| Chain | Residue |
| A | ASP22 |
| A | HOH501 |
| A | HOH528 |
| B | GLU293 |
| B | HIS296 |
| B | ASP298 |
| B | LEU299 |
| A | ALA18 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | binding site for residue TRS A 405 |
| Chain | Residue |
| A | LYS128 |
| A | GLU129 |
| A | GLU130 |
| A | HOH517 |
| A | HOH519 |
| B | HIS54 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | binding site for residue GOL A 406 |
| Chain | Residue |
| A | PRO89 |
| A | MET133 |
| A | PHE135 |
| A | HOH514 |
| A | HOH696 |
| site_id | AC7 |
| Number of Residues | 15 |
| Details | binding site for residue C0A A 407 |
| Chain | Residue |
| A | TYR46 |
| A | ASP48 |
| A | ASP181 |
| A | PHE182 |
| A | CYS215 |
| A | SER216 |
| A | ALA217 |
| A | GLY218 |
| A | ILE219 |
| A | GLY220 |
| A | ARG221 |
| A | GLN262 |
| A | HOH559 |
| A | HOH709 |
| A | HOH770 |
| site_id | AC8 |
| Number of Residues | 2 |
| Details | binding site for residue CL B 401 |
| Chain | Residue |
| B | PRO38 |
| B | LYS39 |
| site_id | AC9 |
| Number of Residues | 3 |
| Details | binding site for residue CL B 402 |
| Chain | Residue |
| B | ARG112 |
| B | VAL113 |
| B | HIS175 |
| site_id | AD1 |
| Number of Residues | 4 |
| Details | binding site for residue TRS B 403 |
| Chain | Residue |
| A | HIS54 |
| B | GLU129 |
| B | GLU130 |
| B | HOH607 |
| site_id | AD2 |
| Number of Residues | 14 |
| Details | binding site for residue C0A B 404 |
| Chain | Residue |
| B | TYR46 |
| B | ASP48 |
| B | ASP181 |
| B | PHE182 |
| B | CYS215 |
| B | SER216 |
| B | ALA217 |
| B | GLY218 |
| B | ILE219 |
| B | GLY220 |
| B | ARG221 |
| B | GLN262 |
| B | HOH584 |
| B | HOH623 |
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 | 2 |
| Details | Active site: {"description":"Phosphocysteine intermediate"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Binding site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 14 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"15592455","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| 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_FI6 |
| 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_FI7 |
| 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_FI8 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine; by CLK1 and CLK2","evidences":[{"source":"PubMed","id":"10480872","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| 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 |
