3ISG
Structure of the class D beta-lactamase OXA-1 in complex with doripenem
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0008658 | molecular_function | penicillin binding |
| A | 0008800 | molecular_function | beta-lactamase activity |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0017001 | biological_process | antibiotic catabolic process |
| A | 0046677 | biological_process | response to antibiotic |
| B | 0008658 | molecular_function | penicillin binding |
| B | 0008800 | molecular_function | beta-lactamase activity |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0017001 | biological_process | antibiotic catabolic process |
| B | 0046677 | biological_process | response to antibiotic |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE DRW A 300 |
| Chain | Residue |
| A | ASP66 |
| A | GLY214 |
| A | ALA215 |
| A | LEU255 |
| A | HOH306 |
| A | HOH357 |
| A | HOH370 |
| A | SER67 |
| A | KCX70 |
| A | MET99 |
| A | SER115 |
| A | VAL117 |
| A | LEU161 |
| A | LYS212 |
| A | THR213 |
| site_id | AC2 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE DRW B 300 |
| Chain | Residue |
| B | ASP66 |
| B | SER67 |
| B | KCX70 |
| B | GLY98 |
| B | MET99 |
| B | SER115 |
| B | VAL117 |
| B | LEU161 |
| B | LYS212 |
| B | THR213 |
| B | GLY214 |
| B | ALA215 |
| B | LEU255 |
| B | SER258 |
| B | HOH276 |
| B | HOH345 |
| B | HOH443 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MPD B 400 |
| Chain | Residue |
| B | ILE82 |
| B | GLU122 |
| B | HOH347 |
Functional Information from PROSITE/UniProt
| site_id | PS00337 |
| Number of Residues | 11 |
| Details | BETA_LACTAMASE_D Beta-lactamase class-D active site. PdSTFKIAlSL |
| Chain | Residue | Details |
| A | PRO65-LEU75 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Acyl-ester intermediate |
| Chain | Residue | Details |
| A | SER67 | |
| B | SER67 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000250 |
| Chain | Residue | Details |
| A | LYS236 | |
| B | LYS236 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | MOD_RES: N6-carboxylysine => ECO:0000269|PubMed:12493831 |
| Chain | Residue | Details |
| A | KCX70 | |
| B | KCX70 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1m6k |
| Chain | Residue | Details |
| A | SER67 |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1m6k |
| Chain | Residue | Details |
| B | SER67 |
| site_id | MCSA1 |
| Number of Residues | 6 |
| Details | M-CSA 210 |
| Chain | Residue | Details |
| A | SER67 | covalently attached, nucleofuge, nucleophile, proton acceptor, proton donor |
| A | KCX70 | proton acceptor, proton donor, proton relay |
| A | SER115 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
| A | SER120 | electrostatic stabiliser, hydrogen bond donor |
| A | TRP160 | electrostatic stabiliser, hydrogen bond donor |
| A | ALA215 | electrostatic stabiliser, hydrogen bond donor |
| site_id | MCSA2 |
| Number of Residues | 6 |
| Details | M-CSA 210 |
| Chain | Residue | Details |
| B | SER67 | covalently attached, nucleofuge, nucleophile, proton acceptor, proton donor |
| B | KCX70 | proton acceptor, proton donor, proton relay |
| B | SER115 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
| B | SER120 | electrostatic stabiliser, hydrogen bond donor |
| B | TRP160 | electrostatic stabiliser, hydrogen bond donor |
| B | ALA215 | electrostatic stabiliser, hydrogen bond donor |
