4MLL
The 1.4 A structure of the class D beta-lactamase OXA-1 K70D complexed with oxacillin
Replaces: 4F7YFunctional 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 | 0042597 | cellular_component | periplasmic space |
| 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 | 0042597 | cellular_component | periplasmic space |
| B | 0046677 | biological_process | response to antibiotic |
| C | 0008658 | molecular_function | penicillin binding |
| C | 0008800 | molecular_function | beta-lactamase activity |
| C | 0016787 | molecular_function | hydrolase activity |
| C | 0042597 | cellular_component | periplasmic space |
| C | 0046677 | biological_process | response to antibiotic |
| D | 0008658 | molecular_function | penicillin binding |
| D | 0008800 | molecular_function | beta-lactamase activity |
| D | 0016787 | molecular_function | hydrolase activity |
| D | 0042597 | cellular_component | periplasmic space |
| D | 0046677 | biological_process | response to antibiotic |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE 1S6 A 301 |
| Chain | Residue |
| A | ASP66 |
| A | LEU255 |
| A | SER258 |
| A | HOH458 |
| A | HOH477 |
| A | HOH502 |
| B | LYS236 |
| B | SER237 |
| B | GLY238 |
| A | SER67 |
| A | MET99 |
| A | TRP102 |
| A | SER115 |
| A | VAL117 |
| A | THR213 |
| A | GLY214 |
| A | ALA215 |
| site_id | AC2 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE PO4 A 302 |
| Chain | Residue |
| A | GLU122 |
| A | HOH620 |
| site_id | AC3 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE PO4 A 303 |
| Chain | Residue |
| A | ASN193 |
| A | GLU196 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE PO4 A 305 |
| Chain | Residue |
| A | ASN250 |
| A | GLY252 |
| B | ASN193 |
| B | GLU196 |
| site_id | AC5 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE MPD A 304 |
| Chain | Residue |
| A | ASN130 |
| A | LYS133 |
| A | HOH632 |
| C | PHE114 |
| C | TYR199 |
| C | LEU200 |
| C | HOH476 |
| C | HOH511 |
| C | HOH624 |
| site_id | AC6 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE 1S6 B 301 |
| Chain | Residue |
| A | LYS236 |
| A | GLY238 |
| A | HOH505 |
| B | ASP66 |
| B | SER67 |
| B | MET99 |
| B | TRP102 |
| B | SER115 |
| B | VAL117 |
| B | GLY214 |
| B | ALA215 |
| B | LEU255 |
| B | SER258 |
| B | HOH414 |
| B | HOH424 |
| B | HOH450 |
| B | HOH452 |
| B | HOH494 |
| B | HOH587 |
| site_id | AC7 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE PO4 B 302 |
| Chain | Residue |
| B | GLU122 |
| B | HOH545 |
| site_id | AC8 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE 1S6 C 301 |
| Chain | Residue |
| C | ASP66 |
| C | SER67 |
| C | TRP102 |
| C | SER115 |
| C | VAL117 |
| C | THR213 |
| C | GLY214 |
| C | ALA215 |
| C | SER258 |
| C | HOH438 |
| C | HOH556 |
| C | HOH576 |
| C | HOH641 |
| D | LYS236 |
| D | GLY238 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PO4 C 302 |
| Chain | Residue |
| C | ASN193 |
| C | GLU196 |
| D | ASN250 |
| D | LEU251 |
| D | GLY252 |
| site_id | BC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE PO4 C 303 |
| Chain | Residue |
| C | ILE82 |
| C | PHE90 |
| D | HOH576 |
| site_id | BC2 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE 1S6 D 301 |
| Chain | Residue |
| C | LYS236 |
| C | SER237 |
| C | GLY238 |
| D | ASP66 |
| D | SER67 |
| D | MET99 |
| D | TRP102 |
| D | SER115 |
| D | VAL117 |
| D | THR213 |
| D | GLY214 |
| D | ALA215 |
| D | LEU255 |
| D | SER258 |
| D | HOH415 |
| D | HOH478 |
| D | HOH490 |
| site_id | BC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE PO4 D 302 |
| Chain | Residue |
| D | GLU122 |
| D | LYS126 |
| D | HOH532 |
| site_id | BC4 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE MPD D 303 |
| Chain | Residue |
| B | TYR199 |
| B | LEU200 |
| B | HOH500 |
| B | HOH569 |
| B | HOH591 |
| D | LYS133 |
| B | GLN113 |
| site_id | BC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MPD D 304 |
| Chain | Residue |
| C | LEU251 |
| C | GLY252 |
| D | GLU192 |
| D | ASN193 |
| D | GLU196 |
| D | HOH619 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | ACT_SITE: Acyl-ester intermediate => ECO:0000255|PROSITE-ProRule:PRU10103, ECO:0000269|PubMed:19919101, ECO:0000269|PubMed:24165180, ECO:0007744|PDB:3ISG, ECO:0007744|PDB:4MLL |
| Chain | Residue | Details |
| A | SER67 | |
| B | SER67 | |
| C | SER67 | |
| D | SER67 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 20 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:19919101, ECO:0000269|PubMed:24165180, ECO:0007744|PDB:3ISG, ECO:0007744|PDB:4MLL |
| Chain | Residue | Details |
| A | SER67 | |
| B | ALA215 | |
| C | SER67 | |
| C | ASP70 | |
| C | SER115 | |
| C | THR213 | |
| C | ALA215 | |
| D | SER67 | |
| D | ASP70 | |
| D | SER115 | |
| D | THR213 | |
| A | ASP70 | |
| D | ALA215 | |
| A | SER115 | |
| A | THR213 | |
| A | ALA215 | |
| B | SER67 | |
| B | ASP70 | |
| B | SER115 | |
| B | THR213 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | MOD_RES: N6-carboxylysine => ECO:0000269|PubMed:12493831, ECO:0000269|PubMed:19919101 |
| Chain | Residue | Details |
| A | ASP70 | |
| B | ASP70 | |
| C | ASP70 | |
| D | ASP70 |
Catalytic Information from CSA
| 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 | ASP70 | 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 | ASP70 | 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 |
| site_id | MCSA3 |
| Number of Residues | 6 |
| Details | M-CSA 210 |
| Chain | Residue | Details |
| C | SER67 | covalently attached, nucleofuge, nucleophile, proton acceptor, proton donor |
| C | ASP70 | proton acceptor, proton donor, proton relay |
| C | SER115 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
| C | SER120 | electrostatic stabiliser, hydrogen bond donor |
| C | TRP160 | electrostatic stabiliser, hydrogen bond donor |
| C | ALA215 | electrostatic stabiliser, hydrogen bond donor |
| site_id | MCSA4 |
| Number of Residues | 6 |
| Details | M-CSA 210 |
| Chain | Residue | Details |
| D | SER67 | covalently attached, nucleofuge, nucleophile, proton acceptor, proton donor |
| D | ASP70 | proton acceptor, proton donor, proton relay |
| D | SER115 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
| D | SER120 | electrostatic stabiliser, hydrogen bond donor |
| D | TRP160 | electrostatic stabiliser, hydrogen bond donor |
| D | ALA215 | electrostatic stabiliser, hydrogen bond donor |
