6B8E
Multiconformer model of apo WT PTP1B with glycerol at 180 K
Functional Information from GO Data
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | binding site for residue GOL A 301 |
| Chain | Residue |
| A | ASP48 |
| A | PHE182 |
| A | ALA217 |
| A | GLN262 |
| A | SER285 |
| A | GOL303 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | binding site for residue GOL A 302 |
| Chain | Residue |
| A | VAL155 |
| A | HOH411 |
| A | HOH472 |
| A | SER146 |
| A | GLU147 |
| A | ASP148 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | binding site for residue GOL A 303 |
| Chain | Residue |
| A | ASP48 |
| A | MET258 |
| A | GLY259 |
| A | GOL301 |
| A | GOL304 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | binding site for residue GOL A 304 |
| Chain | Residue |
| A | SER28 |
| A | ASP29 |
| A | MET258 |
| A | GOL303 |
| A | HOH434 |
| A | HOH508 |
| A | HOH535 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | binding site for residue TRS A 305 |
| Chain | Residue |
| A | HIS54 |
| A | GLU129 |
| A | GLU130 |
| A | HOH407 |
| A | HOH464 |
| A | HOH489 |
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 | 274 |
| 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 | 1 |
| Details | Active site: {"description":"Phosphocysteine intermediate"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Binding site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 7 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"15592455","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| 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_FI7 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphotyrosine; by EGFR","evidences":[{"source":"PubMed","id":"9355745","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 1 |
| 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_FI9 |
| 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_FI10 |
| Number of Residues | 2 |
| 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 |
