1Z9H
Microsomal prostaglandin E synthase type-2
Functional Information from GO Data
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL D 378 |
| Chain | Residue |
| A | ARG137 |
| A | ARG146 |
| D | TYR287 |
| site_id | AC2 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE ACT A 378 |
| Chain | Residue |
| A | MET286 |
| site_id | AC3 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL B 378 |
| Chain | Residue |
| B | ARG137 |
| C | TYR287 |
| site_id | AC4 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE ACT B 379 |
| Chain | Residue |
| B | MET286 |
| site_id | AC5 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL B 380 |
| Chain | Residue |
| B | TYR287 |
| C | ARG137 |
| site_id | AC6 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE ACT C 378 |
| Chain | Residue |
| C | MET286 |
| site_id | AC7 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL D 475 |
| Chain | Residue |
| A | TYR287 |
| D | ARG137 |
| site_id | AC8 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE ACT D 477 |
| Chain | Residue |
| D | MET286 |
| site_id | AC9 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE IMN A 379 |
| Chain | Residue |
| A | TYR107 |
| A | THR109 |
| A | CYS110 |
| A | PRO111 |
| A | PHE112 |
| A | PRO134 |
| A | ILE246 |
| A | VAL250 |
| A | TYR251 |
| A | SER260 |
| A | TYR263 |
| A | ILE264 |
| A | VAL343 |
| A | LEU347 |
| site_id | BC1 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE IMN B 381 |
| Chain | Residue |
| B | HOH2 |
| B | TYR107 |
| B | THR109 |
| B | CYS110 |
| B | PRO111 |
| B | PHE112 |
| B | PRO134 |
| B | ILE246 |
| B | VAL250 |
| B | TYR251 |
| B | SER260 |
| B | TYR263 |
| B | ILE264 |
| B | VAL343 |
| B | LEU347 |
| site_id | BC2 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE IMN C 379 |
| Chain | Residue |
| C | TYR107 |
| C | THR109 |
| C | CYS110 |
| C | PRO111 |
| C | PHE112 |
| C | PRO134 |
| C | ILE246 |
| C | VAL250 |
| C | TYR251 |
| C | SER260 |
| C | TYR263 |
| C | ILE264 |
| C | VAL343 |
| C | LEU347 |
| site_id | BC3 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE IMN D 476 |
| Chain | Residue |
| D | TYR107 |
| D | THR109 |
| D | CYS110 |
| D | PRO111 |
| D | PHE112 |
| D | PRO134 |
| D | ILE246 |
| D | VAL250 |
| D | TYR251 |
| D | SER260 |
| D | TYR263 |
| D | ILE264 |
| D | VAL343 |
| D | LEU347 |
| D | HOH478 |
Functional Information from PROSITE/UniProt
| site_id | PS00195 |
| Number of Residues | 17 |
| Details | GLUTAREDOXIN_1 Glutaredoxin active site. LYqyktCPFCskVrafL |
| Chain | Residue | Details |
| A | LEU104-LEU120 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:17585783 |
| Chain | Residue | Details |
| A | VAL148 | |
| A | ASP164 | |
| B | VAL148 | |
| B | ASP164 | |
| C | VAL148 | |
| C | ASP164 | |
| D | VAL148 | |
| D | ASP164 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q9H7Z7 |
| Chain | Residue | Details |
| A | SER95 | |
| B | SER95 | |
| C | SER95 | |
| D | SER95 |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 4 |
| Details | M-CSA 192 |
| Chain | Residue | Details |
| A | TYR107 | activator, electrostatic stabiliser, hydrogen bond donor |
| A | CYS110 | hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor |
| A | PHE112 | electrostatic stabiliser, hydrogen bond donor |
| A | CYS113 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, increase acidity |
| site_id | MCSA2 |
| Number of Residues | 4 |
| Details | M-CSA 192 |
| Chain | Residue | Details |
| B | TYR107 | activator, electrostatic stabiliser, hydrogen bond donor |
| B | CYS110 | hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor |
| B | PHE112 | electrostatic stabiliser, hydrogen bond donor |
| B | CYS113 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, increase acidity |
| site_id | MCSA3 |
| Number of Residues | 4 |
| Details | M-CSA 192 |
| Chain | Residue | Details |
| C | TYR107 | activator, electrostatic stabiliser, hydrogen bond donor |
| C | CYS110 | hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor |
| C | PHE112 | electrostatic stabiliser, hydrogen bond donor |
| C | CYS113 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, increase acidity |
| site_id | MCSA4 |
| Number of Residues | 4 |
| Details | M-CSA 192 |
| Chain | Residue | Details |
| D | TYR107 | activator, electrostatic stabiliser, hydrogen bond donor |
| D | CYS110 | hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor |
| D | PHE112 | electrostatic stabiliser, hydrogen bond donor |
| D | CYS113 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, increase acidity |
