1M6K
Structure of the OXA-1 class D beta-lactamase
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 | 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 | 0017001 | biological_process | antibiotic catabolic process |
| B | 0042597 | cellular_component | periplasmic space |
| B | 0046677 | biological_process | response to antibiotic |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MPD A 401 |
| Chain | Residue |
| A | VAL117 |
| A | ALA215 |
| A | HOH502 |
| A | HOH934 |
| B | SER237 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MPD B 402 |
| Chain | Residue |
| B | HOH877 |
| A | SER237 |
| B | VAL117 |
| B | ALA215 |
| B | HOH503 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE MPD A 403 |
| Chain | Residue |
| A | ILE82 |
| A | PHE90 |
| A | GLU122 |
| A | LYS126 |
| A | HOH894 |
| A | HOH974 |
| B | HOH762 |
| site_id | AC4 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE MPD B 404 |
| Chain | Residue |
| B | GLU122 |
| B | HOH956 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MPD A 405 |
| Chain | Residue |
| A | PHE114 |
| A | GLY142 |
| A | ASN143 |
| A | HOH701 |
| site_id | AC6 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE MPD A 406 |
| Chain | Residue |
| A | ASN193 |
| B | LEU251 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MPD B 407 |
| Chain | Residue |
| B | PHE114 |
| B | GLY142 |
| B | ASN143 |
| B | HOH768 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MPD A 408 |
| Chain | Residue |
| A | ASN183 |
| A | LEU184 |
| A | PRO185 |
| B | ARG222 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MPD A 409 |
| Chain | Residue |
| A | LYS187 |
| A | ASN188 |
| A | HOH683 |
| A | HOH717 |
| site_id | BC1 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE MPD B 410 |
| Chain | Residue |
| A | LYS236 |
| A | SER237 |
| A | HOH710 |
| B | VAL117 |
| B | GLN121 |
| B | GLU158 |
| B | LEU161 |
| B | HOH787 |
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 | Active site: {"description":"Acyl-ester intermediate","evidences":[{"source":"PROSITE-ProRule","id":"PRU10103","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"19919101","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24165180","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3ISG","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4MLL","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 10 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"19919101","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24165180","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3ISG","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4MLL","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-carboxylysine","evidences":[{"source":"PubMed","id":"12493831","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19919101","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | a catalytic site defined by CSA, PubMed 12493831 |
| Chain | Residue | Details |
| A | SER67 | |
| A | SER67 |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | a catalytic site defined by CSA, PubMed 12493831 |
| 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 | VAL119 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
| A | THR124 | electrostatic stabiliser, hydrogen bond donor |
| A | SER164 | electrostatic stabiliser, hydrogen bond donor |
| A | ALA220 | 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 | VAL119 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
| B | THR124 | electrostatic stabiliser, hydrogen bond donor |
| B | SER164 | electrostatic stabiliser, hydrogen bond donor |
| B | ALA220 | electrostatic stabiliser, hydrogen bond donor |
