1EEO
CRYSTAL STRUCTURE OF PROTEIN TYROSINE PHOSPHATASE 1B COMPLEXED WITH ACETYL-E-L-E-F-PTYR-M-D-Y-E-NH2
Functional Information from GO Data
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE MG A 322 |
| Chain | Residue |
| A | HOH485 |
| site_id | AC2 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR CHAIN B OF ACETYL-E-L-E-F-PTYR-M-D-Y-E-NH2 PEPTIDE |
| Chain | Residue |
| A | PHE182 |
| A | SER215 |
| A | SER216 |
| A | ALA217 |
| A | GLY218 |
| A | ILE219 |
| A | GLY220 |
| A | ARG221 |
| A | LYS247 |
| A | GLN262 |
| A | GLN9 |
| A | HOH367 |
| A | HOH418 |
| B | HOH12 |
| B | HOH124 |
| B | HOH129 |
| B | HOH151 |
| B | HOH154 |
| A | ILE10 |
| A | ALA18 |
| A | ILE19 |
| A | ARG45 |
| A | TYR46 |
| A | ARG47 |
| A | ASP48 |
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 | CSA1 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1bzc |
| Chain | Residue | Details |
| A | ARG221 | |
| A | ASP181 | |
| A | SER215 | |
| A | SER222 |
| site_id | MCSA1 |
| Number of Residues | 5 |
| Details | M-CSA 469 |
| Chain | Residue | Details |
| A | ASP181 | proton shuttle (general acid/base) |
| A | SER215 | covalent catalysis |
| A | ARG221 | activator, electrostatic stabiliser |
| A | SER222 | activator, electrostatic stabiliser |
| A | GLN262 | steric role |
