5J8R
Crystal Structure of the Catalytic Domain of Human Protein Tyrosine Phosphatase non-receptor Type 12 - K61R mutant
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004725 | molecular_function | protein tyrosine phosphatase activity |
| A | 0004726 | molecular_function | non-membrane spanning protein tyrosine phosphatase activity |
| A | 0006470 | biological_process | protein dephosphorylation |
| A | 0016311 | biological_process | dephosphorylation |
| B | 0004725 | molecular_function | protein tyrosine phosphatase activity |
| B | 0004726 | molecular_function | non-membrane spanning protein tyrosine phosphatase activity |
| B | 0006470 | biological_process | protein dephosphorylation |
| B | 0016311 | biological_process | dephosphorylation |
| C | 0004725 | molecular_function | protein tyrosine phosphatase activity |
| C | 0004726 | molecular_function | non-membrane spanning protein tyrosine phosphatase activity |
| C | 0006470 | biological_process | protein dephosphorylation |
| C | 0016311 | biological_process | dephosphorylation |
| D | 0004725 | molecular_function | protein tyrosine phosphatase activity |
| D | 0004726 | molecular_function | non-membrane spanning protein tyrosine phosphatase activity |
| D | 0006470 | biological_process | protein dephosphorylation |
| D | 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. IHCsaGcgRTG |
| Chain | Residue | Details |
| A | ILE229-GLY239 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | ACT_SITE: Phosphocysteine intermediate => ECO:0000255|PROSITE-ProRule:PRU00160, ECO:0000255|PROSITE-ProRule:PRU10044 |
| Chain | Residue | Details |
| A | CYS231 | |
| B | CYS231 | |
| C | CYS231 | |
| D | CYS231 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 16 |
| Details | BINDING: BINDING => ECO:0000305|PubMed:27134172 |
| Chain | Residue | Details |
| A | ARG36 | |
| C | ARG63 | |
| C | ASP199 | |
| C | GLN278 | |
| D | ARG36 | |
| D | ARG63 | |
| D | ASP199 | |
| D | GLN278 | |
| A | ARG63 | |
| A | ASP199 | |
| A | GLN278 | |
| B | ARG36 | |
| B | ARG63 | |
| B | ASP199 | |
| B | GLN278 | |
| C | ARG36 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000250 |
| Chain | Residue | Details |
| A | CYS231 | |
| B | CYS231 | |
| C | CYS231 | |
| D | CYS231 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | MOD_RES: N-acetylmethionine => ECO:0000269|PubMed:12665801, ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378 |
| Chain | Residue | Details |
| A | MET1 | |
| B | MET1 | |
| C | MET1 | |
| D | MET1 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphoserine => ECO:0000269|PubMed:27134172, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163 |
| Chain | Residue | Details |
| A | SER19 | |
| B | SER19 | |
| C | SER19 | |
| D | SER19 |
