3ZMP
Src-derived peptide inhibitor complex of PTP1B
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 SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | MOD_RES: Phosphotyrosine; by CSK => ECO:0000269|PubMed:19307596, ECO:0000269|PubMed:26936507, ECO:0000269|PubMed:7525268, ECO:0000269|PubMed:7929427, ECO:0007744|PubMed:19369195 |
Chain | Residue | Details |
C | FTY4 | |
D | FTY4 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | BINDING: |
Chain | Residue | Details |
A | ASP181 | |
B | ASP181 |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000250 |
Chain | Residue | Details |
A | SER215 | |
A | GLN262 | |
B | SER215 | |
B | GLN262 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | MOD_RES: N-acetylmethionine => ECO:0000269|PubMed:2546149 |
Chain | Residue | Details |
A | MET1 | |
B | MET1 |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | MOD_RES: Phosphotyrosine => ECO:0007744|PubMed:15592455 |
Chain | Residue | Details |
A | TYR20 | |
B | TYR20 |
site_id | SWS_FT_FI6 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine; by PKB/AKT1, CLK1 and CLK2 => ECO:0000269|PubMed:10480872, ECO:0000269|PubMed:11579209, ECO:0007744|PubMed:23186163 |
Chain | Residue | Details |
A | SER50 | |
B | SER50 |
site_id | SWS_FT_FI7 |
Number of Residues | 2 |
Details | MOD_RES: Phosphotyrosine; by EGFR => ECO:0000269|PubMed:9355745 |
Chain | Residue | Details |
A | TYR66 | |
B | TYR66 |
site_id | SWS_FT_FI8 |
Number of Residues | 2 |
Details | MOD_RES: S-nitrosocysteine; in reversibly inhibited form => ECO:0000269|PubMed:22169477 |
Chain | Residue | Details |
A | SER215 | |
B | SER215 |
site_id | SWS_FT_FI9 |
Number of Residues | 4 |
Details | MOD_RES: Phosphoserine; by CLK1 and CLK2 => ECO:0000269|PubMed:10480872 |
Chain | Residue | Details |
A | SER242 | |
A | SER243 | |
B | SER242 | |
B | SER243 |
site_id | SWS_FT_FI10 |
Number of Residues | 4 |
Details | CROSSLNK: N,N-(cysteine-1,S-diyl)serine (Cys-Ser); in inhibited form => ECO:0000269|PubMed:12802338, ECO:0000269|PubMed:12802339 |
Chain | Residue | Details |
A | SER215 | |
A | SER216 | |
B | SER215 | |
B | SER216 |
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 | SER215 | 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 | SER215 | covalent catalysis |
B | ARG221 | activator, electrostatic stabiliser |
B | SER222 | activator, electrostatic stabiliser |
B | GLN262 | steric role |