2HVL
Crystal structure of the HePTP catalytic domain C270S mutant
Functional Information from GO Data
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE PO4 A 340 |
Chain | Residue |
A | SER270 |
A | HOH461 |
A | SER271 |
A | ALA272 |
A | GLY273 |
A | ILE274 |
A | GLY275 |
A | ARG276 |
A | GLN314 |
A | HOH403 |
site_id | AC2 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE PO4 A 341 |
Chain | Residue |
A | THR174 |
A | GLN175 |
A | SER271 |
A | ARG276 |
A | HOH434 |
A | HOH441 |
A | HOH603 |
A | HOH614 |
site_id | AC3 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL A 401 |
Chain | Residue |
A | GLN112 |
A | SER113 |
A | TYR133 |
A | GLU141 |
A | HOH407 |
A | HOH511 |
A | HOH588 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | ACT_SITE: Phosphocysteine intermediate => ECO:0000255|PROSITE-ProRule:PRU00160, ECO:0000255|PROSITE-ProRule:PRU10044, ECO:0000269|PubMed:9624114 |
Chain | Residue | Details |
A | SER270 |
site_id | SWS_FT_FI2 |
Number of Residues | 3 |
Details | BINDING: |
Chain | Residue | Details |
A | ASP236 | |
A | SER270 | |
A | GLN314 |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | MOD_RES: Phosphothreonine => ECO:0000269|PubMed:10206983, ECO:0007744|PubMed:18088087, ECO:0007744|PubMed:23186163 |
Chain | Residue | Details |
A | THR45 |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0000269|PubMed:10206983 |
Chain | Residue | Details |
A | SER72 |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163 |
Chain | Residue | Details |
A | SER89 |
site_id | SWS_FT_FI6 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163 |
Chain | Residue | Details |
A | SER122 |
site_id | SWS_FT_FI7 |
Number of Residues | 1 |
Details | MOD_RES: Cysteine sulfenic acid (-SOH) => ECO:0000250 |
Chain | Residue | Details |
A | SER270 |