6V1O
Structure of OXA-48 bound to QPX7728 at 1.80 A
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005886 | cellular_component | plasma membrane |
| 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 |
| A | 0071555 | biological_process | cell wall organization |
| B | 0005886 | cellular_component | plasma membrane |
| 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 |
| B | 0071555 | biological_process | cell wall organization |
| C | 0005886 | cellular_component | plasma membrane |
| C | 0008658 | molecular_function | penicillin binding |
| C | 0008800 | molecular_function | beta-lactamase activity |
| C | 0016787 | molecular_function | hydrolase activity |
| C | 0017001 | biological_process | antibiotic catabolic process |
| C | 0046677 | biological_process | response to antibiotic |
| C | 0071555 | biological_process | cell wall organization |
| D | 0005886 | cellular_component | plasma membrane |
| D | 0008658 | molecular_function | penicillin binding |
| D | 0008800 | molecular_function | beta-lactamase activity |
| D | 0016787 | molecular_function | hydrolase activity |
| D | 0017001 | biological_process | antibiotic catabolic process |
| D | 0046677 | biological_process | response to antibiotic |
| D | 0071555 | biological_process | cell wall organization |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 13 |
| Details | binding site for residue RM9 A 301 |
| Chain | Residue |
| A | ALA69 |
| A | TYR211 |
| A | LEU247 |
| A | ARG250 |
| A | HOH522 |
| A | SER70 |
| A | KCX73 |
| A | TRP105 |
| A | SER118 |
| A | VAL120 |
| A | LYS208 |
| A | THR209 |
| A | GLY210 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | binding site for residue MG A 302 |
| Chain | Residue |
| A | GLU37 |
| A | GLU256 |
| A | HOH403 |
| A | HOH456 |
| A | HOH576 |
| A | HOH623 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | binding site for residue MG A 303 |
| Chain | Residue |
| A | ASP143 |
| A | GLU147 |
| A | HOH471 |
| A | HOH492 |
| A | HOH499 |
| A | HOH539 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | binding site for residue CL A 304 |
| Chain | Residue |
| A | ARG206 |
| A | HOH666 |
| B | ARG206 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | binding site for residue MG B 302 |
| Chain | Residue |
| B | ASP143 |
| B | GLU147 |
| B | HOH404 |
| B | HOH438 |
| B | HOH535 |
| B | HOH537 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | binding site for residue MG B 303 |
| Chain | Residue |
| B | GLU37 |
| B | GLU256 |
| B | HOH410 |
| B | HOH479 |
| B | HOH485 |
| B | HOH591 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | binding site for residue MG C 302 |
| Chain | Residue |
| C | ASP143 |
| C | GLU147 |
| C | HOH414 |
| C | HOH467 |
| C | HOH515 |
| C | HOH577 |
| site_id | AC8 |
| Number of Residues | 2 |
| Details | binding site for residue CL C 303 |
| Chain | Residue |
| C | ARG206 |
| D | ARG206 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | binding site for residue MG D 302 |
| Chain | Residue |
| D | ASP143 |
| D | GLU147 |
| D | HOH436 |
| D | HOH492 |
| D | HOH520 |
| D | HOH551 |
| site_id | AD1 |
| Number of Residues | 5 |
| Details | binding site for residue MG D 303 |
| Chain | Residue |
| C | HOH437 |
| C | HOH708 |
| D | HOH422 |
| D | HOH658 |
| D | HOH704 |
| site_id | AD2 |
| Number of Residues | 5 |
| Details | binding site for residue MG D 304 |
| Chain | Residue |
| D | HIS140 |
| D | HOH501 |
| D | HOH530 |
| D | HOH564 |
| D | HOH665 |
| site_id | AD3 |
| Number of Residues | 15 |
| Details | binding site for Di-peptide RM9 B 301 and SER B 70 |
| Chain | Residue |
| B | PRO68 |
| B | ALA69 |
| B | THR71 |
| B | PHE72 |
| B | KCX73 |
| B | TRP105 |
| B | SER118 |
| B | VAL120 |
| B | LYS208 |
| B | THR209 |
| B | GLY210 |
| B | TYR211 |
| B | LEU247 |
| B | ARG250 |
| B | HOH482 |
| site_id | AD4 |
| Number of Residues | 15 |
| Details | binding site for Di-peptide RM9 C 301 and SER C 70 |
| Chain | Residue |
| C | PRO68 |
| C | ALA69 |
| C | THR71 |
| C | PHE72 |
| C | KCX73 |
| C | TRP105 |
| C | SER118 |
| C | VAL120 |
| C | LYS208 |
| C | THR209 |
| C | GLY210 |
| C | TYR211 |
| C | LEU247 |
| C | ARG250 |
| C | HOH413 |
| site_id | AD5 |
| Number of Residues | 14 |
| Details | binding site for Di-peptide RM9 D 301 and SER D 70 |
| Chain | Residue |
| D | TRP105 |
| D | SER118 |
| D | VAL120 |
| D | LYS208 |
| D | THR209 |
| D | GLY210 |
| D | TYR211 |
| D | ARG250 |
| D | HOH531 |
| D | PRO68 |
| D | ALA69 |
| D | THR71 |
| D | PHE72 |
| D | KCX73 |
Functional Information from PROSITE/UniProt
| site_id | PS00337 |
| Number of Residues | 11 |
| Details | BETA_LACTAMASE_D Beta-lactamase class-D active site. PaSTFKIPnSL |
| Chain | Residue | Details |
| A | PRO68-LEU78 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | Active site: {"description":"Acyl-ester intermediate","evidences":[{"source":"PIRSR","id":"PIRSR602137-50","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"25406838","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"26731698","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"31358584","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"32150407","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4WMC","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5FAQ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5FAS","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6P97","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6P98","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6P99","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6P9C","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6V1O","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"N6-carboxylysine","evidences":[{"source":"PIRSR","id":"PIRSR602137-50","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"19477418","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25406838","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3HBR","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4WMC","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 12 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"Q8RLA6","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P13661","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |






