6PT5
Crystal Structure of Class D Beta-lactamase OXA-48 with Cefoxitin
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 | 2 |
Details | binding site for residue CL A 301 |
Chain | Residue |
A | ARG206 |
C | ARG206 |
site_id | AC2 |
Number of Residues | 11 |
Details | binding site for residue 1S7 A 302 |
Chain | Residue |
A | TYR211 |
A | THR213 |
A | ARG214 |
A | ARG250 |
A | SER70 |
A | TRP105 |
A | SER118 |
A | VAL120 |
A | LEU158 |
A | THR209 |
A | GLY210 |
site_id | AC3 |
Number of Residues | 2 |
Details | binding site for residue CL B 301 |
Chain | Residue |
B | ARG206 |
D | ARG206 |
site_id | AC4 |
Number of Residues | 15 |
Details | binding site for Di-peptide 1S7 B 302 and SER B 70 |
Chain | Residue |
B | PRO68 |
B | ALA69 |
B | THR71 |
B | PHE72 |
B | LYS73 |
B | SER118 |
B | VAL120 |
B | LEU158 |
B | LYS208 |
B | THR209 |
B | GLY210 |
B | TYR211 |
B | THR213 |
B | ARG214 |
B | ARG250 |
site_id | AC5 |
Number of Residues | 18 |
Details | binding site for Di-peptide 1S7 B 302 and ARG B 250 |
Chain | Residue |
B | ALA69 |
B | SER70 |
B | SER118 |
B | VAL120 |
B | LEU158 |
B | THR209 |
B | GLY210 |
B | TYR211 |
B | THR213 |
B | ARG214 |
B | TRP221 |
B | MET237 |
B | LEU247 |
B | GLY248 |
B | LEU249 |
B | GLN251 |
B | ALA252 |
B | THR254 |
site_id | AC6 |
Number of Residues | 18 |
Details | binding site for Di-peptide 1S7 C 301 and ARG C 250 |
Chain | Residue |
C | ALA69 |
C | SER70 |
C | SER118 |
C | VAL120 |
C | LEU158 |
C | THR209 |
C | GLY210 |
C | TYR211 |
C | SER212 |
C | THR213 |
C | ARG214 |
C | TRP221 |
C | LEU247 |
C | GLY248 |
C | LEU249 |
C | GLN251 |
C | ALA252 |
C | THR254 |
site_id | AC7 |
Number of Residues | 16 |
Details | binding site for Di-peptide 1S7 C 301 and SER C 70 |
Chain | Residue |
C | PRO68 |
C | ALA69 |
C | THR71 |
C | PHE72 |
C | LYS73 |
C | SER118 |
C | VAL120 |
C | LEU158 |
C | LYS208 |
C | THR209 |
C | GLY210 |
C | TYR211 |
C | SER212 |
C | THR213 |
C | ARG214 |
C | ARG250 |
site_id | AC8 |
Number of Residues | 15 |
Details | binding site for Di-peptide 1S7 D 301 and SER D 70 |
Chain | Residue |
D | PRO68 |
D | ALA69 |
D | THR71 |
D | PHE72 |
D | LYS73 |
D | SER118 |
D | VAL120 |
D | LEU158 |
D | LYS208 |
D | THR209 |
D | GLY210 |
D | TYR211 |
D | THR213 |
D | ARG214 |
D | ARG250 |
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_FI2 |
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_FI3 |
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_FI4 |
Number of Residues | 12 |
Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"Q8RLA6","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI5 |
Number of Residues | 4 |
Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P13661","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |