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 |