6ZZ4
Crystal structure of the PTPN2 C216G mutant
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 PDB Data
site_id | AC1 |
Number of Residues | 12 |
Details | binding site for residue PO4 A 401 |
Chain | Residue |
A | ASP182 |
A | GLN260 |
A | HOH514 |
A | HOH530 |
A | GLY216 |
A | SER217 |
A | ALA218 |
A | GLY219 |
A | ILE220 |
A | GLY221 |
A | ARG222 |
A | SER223 |
site_id | AC2 |
Number of Residues | 3 |
Details | binding site for residue PO4 A 402 |
Chain | Residue |
A | THR155 |
A | HIS157 |
A | HIS176 |
site_id | AC3 |
Number of Residues | 4 |
Details | binding site for residue PO4 A 403 |
Chain | Residue |
A | GLY203 |
A | ASN206 |
A | ASP208 |
A | HIS209 |
site_id | AC4 |
Number of Residues | 12 |
Details | binding site for residue PO4 B 401 |
Chain | Residue |
B | ASP182 |
B | GLY216 |
B | SER217 |
B | ALA218 |
B | GLY219 |
B | ILE220 |
B | GLY221 |
B | ARG222 |
B | SER223 |
B | GLN260 |
B | HOH510 |
B | HOH522 |
site_id | AC5 |
Number of Residues | 6 |
Details | binding site for residue PO4 B 402 |
Chain | Residue |
A | HOH509 |
B | GLU148 |
B | THR155 |
B | HIS157 |
B | HIS176 |
B | HOH554 |
site_id | AC6 |
Number of Residues | 4 |
Details | binding site for residue PO4 B 403 |
Chain | Residue |
B | GLU41 |
B | ASN44 |
B | ARG45 |
B | ASN92 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | ACT_SITE: Phosphocysteine intermediate => ECO:0000255|PROSITE-ProRule:PRU00160, ECO:0000255|PROSITE-ProRule:PRU10044 |
Chain | Residue | Details |
B | GLY216 | |
A | GLY216 |
site_id | SWS_FT_FI2 |
Number of Residues | 6 |
Details | BINDING: BINDING => ECO:0000250 |
Chain | Residue | Details |
B | GLY216 | |
B | GLN260 | |
A | GLN260 | |
B | ASP182 | |
A | ASP182 | |
A | GLY216 |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P18031 |
Chain | Residue | Details |
B | TYR22 | |
B | TYR68 | |
A | TYR22 | |
A | TYR68 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P18031 |
Chain | Residue | Details |
A | SER52 | |
B | SER52 |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | MOD_RES: S-nitrosocysteine => ECO:0000250|UniProtKB:P18031 |
Chain | Residue | Details |
B | GLY216 | |
A | GLY216 |
site_id | SWS_FT_FI6 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163 |
Chain | Residue | Details |
A | SER293 | |
B | SER293 |
site_id | SWS_FT_FI7 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569 |
Chain | Residue | Details |
A | SER298 | |
B | SER298 |
site_id | SWS_FT_FI8 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569 |
Chain | Residue | Details |
A | SER304 | |
B | SER304 |