3HBR
Crystal structure of OXA-48 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 | 0017001 | biological_process | antibiotic catabolic process |
| B | 0008658 | molecular_function | penicillin binding |
| B | 0008800 | molecular_function | beta-lactamase activity |
| B | 0017001 | biological_process | antibiotic catabolic process |
| C | 0008658 | molecular_function | penicillin binding |
| C | 0008800 | molecular_function | beta-lactamase activity |
| C | 0017001 | biological_process | antibiotic catabolic process |
| D | 0008658 | molecular_function | penicillin binding |
| D | 0008800 | molecular_function | beta-lactamase activity |
| D | 0017001 | biological_process | antibiotic catabolic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO A 266 |
| Chain | Residue |
| A | GLU198 |
| A | ALA199 |
| A | ASN200 |
| B | ALA199 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO B 266 |
| Chain | Residue |
| B | HOH456 |
| B | THR197 |
| B | GLU198 |
| B | TRP222 |
| B | GLN251 |
| B | LYS255 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO B 267 |
| Chain | Residue |
| B | TRP25 |
| B | TRP47 |
| B | HOH399 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO C 266 |
| Chain | Residue |
| C | PHE142 |
| C | ASP143 |
| C | SER171 |
| C | PHE172 |
| C | LYS175 |
| C | HOH286 |
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 | 12 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"Q8RLA6","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P13661","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| 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 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1btl |
| Chain | Residue | Details |
| A | SER118 | |
| A | ASP148 | |
| A | SER70 |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1btl |
| Chain | Residue | Details |
| B | SER118 | |
| B | ASP148 | |
| B | SER70 |
| site_id | CSA3 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1btl |
| Chain | Residue | Details |
| C | SER118 | |
| C | ASP148 | |
| C | SER70 |
| site_id | CSA4 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1btl |
| Chain | Residue | Details |
| D | SER118 | |
| D | ASP148 | |
| D | SER70 |
| site_id | CSA5 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1btl |
| Chain | Residue | Details |
| A | SER70 |
| site_id | CSA6 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1btl |
| Chain | Residue | Details |
| B | SER70 |
| site_id | CSA7 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1btl |
| Chain | Residue | Details |
| C | SER70 |
| site_id | CSA8 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1btl |
| Chain | Residue | Details |
| D | SER70 |
