5QB1
OXA-48 IN COMPLEX WITH COMPOUND 36
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 |
| D | ARG206 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | binding site for residue EDO A 302 |
| Chain | Residue |
| A | LEU81 |
| A | SER184 |
| A | ARG186 |
| A | SER187 |
| A | HOH404 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | binding site for residue EDO A 303 |
| Chain | Residue |
| A | VAL232 |
| A | HOH406 |
| D | HIS90 |
| D | GLN193 |
| D | HOH440 |
| A | TYR177 |
| A | GLU227 |
| site_id | AC4 |
| Number of Residues | 9 |
| Details | binding site for residue F1C B 301 |
| Chain | Residue |
| B | SER70 |
| B | VAL120 |
| B | THR209 |
| B | THR213 |
| B | ARG214 |
| B | SER244 |
| B | LEU247 |
| B | ARG250 |
| B | HOH437 |
| site_id | AC5 |
| Number of Residues | 1 |
| Details | binding site for residue CL B 302 |
| Chain | Residue |
| B | ARG206 |
| site_id | AC6 |
| Number of Residues | 1 |
| Details | binding site for residue EDO B 303 |
| Chain | Residue |
| B | LYS116 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | binding site for residue EDO B 304 |
| Chain | Residue |
| B | TYR177 |
| B | GLU227 |
| B | VAL232 |
| B | HOH418 |
| B | HOH426 |
| site_id | AC8 |
| Number of Residues | 2 |
| Details | binding site for residue EDO B 305 |
| Chain | Residue |
| B | ARG107 |
| B | ASN110 |
| site_id | AC9 |
| Number of Residues | 3 |
| Details | binding site for residue EDO C 301 |
| Chain | Residue |
| C | LYS116 |
| C | HOH407 |
| C | HOH434 |
| site_id | AD1 |
| Number of Residues | 3 |
| Details | binding site for residue EDO C 302 |
| Chain | Residue |
| C | SER171 |
| C | ARG174 |
| C | HOH437 |
| site_id | AD2 |
| Number of Residues | 9 |
| Details | binding site for residue F1C D 301 |
| Chain | Residue |
| D | SER70 |
| D | VAL120 |
| D | THR209 |
| D | TYR211 |
| D | ARG214 |
| D | SER244 |
| D | LEU247 |
| D | ARG250 |
| D | HOH401 |
| site_id | AD3 |
| Number of Residues | 5 |
| Details | binding site for residue EDO D 302 |
| Chain | Residue |
| A | ASN200 |
| A | ASP229 |
| D | LYS116 |
| D | HOH418 |
| D | HOH441 |
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 |
