5QAA
OXA-48 IN COMPLEX WITH COMPOUND 6a
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 | 9 |
| Details | binding site for residue EAJ A 301 |
| Chain | Residue |
| A | ILE102 |
| A | THR209 |
| A | TYR211 |
| A | ARG250 |
| A | HOH401 |
| A | HOH404 |
| A | HOH436 |
| A | HOH661 |
| A | HOH676 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | binding site for residue CL A 302 |
| Chain | Residue |
| A | ARG206 |
| A | HOH642 |
| C | ARG206 |
| C | HOH620 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | binding site for residue EDO A 303 |
| Chain | Residue |
| A | ARG100 |
| A | HOH406 |
| A | HOH498 |
| A | HOH566 |
| A | HOH581 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | binding site for residue EDO A 304 |
| Chain | Residue |
| A | SER40 |
| A | ASP240 |
| A | MET241 |
| A | PRO242 |
| A | HOH421 |
| A | HOH488 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | binding site for residue EAJ B 301 |
| Chain | Residue |
| B | THR209 |
| B | TYR211 |
| B | ARG250 |
| B | HOH427 |
| site_id | AC6 |
| Number of Residues | 2 |
| Details | binding site for residue CL B 302 |
| Chain | Residue |
| B | ARG206 |
| B | HOH644 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | binding site for residue EDO B 303 |
| Chain | Residue |
| B | SER184 |
| B | ARG186 |
| B | SER187 |
| B | HOH470 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | binding site for residue EDO B 304 |
| Chain | Residue |
| B | THR167 |
| B | ILE170 |
| B | SER171 |
| B | ARG174 |
| B | HOH403 |
| site_id | AC9 |
| Number of Residues | 7 |
| Details | binding site for residue EDO B 305 |
| Chain | Residue |
| B | LYS39 |
| B | SER40 |
| B | ASP240 |
| B | MET241 |
| B | PRO242 |
| B | HOH422 |
| B | HOH570 |
| site_id | AD1 |
| Number of Residues | 6 |
| Details | binding site for residue EDO B 306 |
| Chain | Residue |
| B | ALA65 |
| B | PHE66 |
| B | PRO217 |
| B | HOH413 |
| B | HOH495 |
| B | HOH513 |
| site_id | AD2 |
| Number of Residues | 10 |
| Details | binding site for residue EAJ C 301 |
| Chain | Residue |
| C | ILE102 |
| C | TYR211 |
| C | LEU247 |
| C | ARG250 |
| C | HOH406 |
| C | HOH407 |
| C | HOH451 |
| C | HOH509 |
| C | HOH511 |
| C | HOH668 |
| site_id | AD3 |
| Number of Residues | 4 |
| Details | binding site for residue EDO C 302 |
| Chain | Residue |
| C | ILE170 |
| C | SER171 |
| C | ARG174 |
| C | HOH542 |
| site_id | AD4 |
| Number of Residues | 7 |
| Details | binding site for residue EDO C 303 |
| Chain | Residue |
| A | HIS90 |
| A | HOH469 |
| C | TYR177 |
| C | GLU227 |
| C | VAL232 |
| C | HOH418 |
| C | HOH456 |
| site_id | AD5 |
| Number of Residues | 4 |
| Details | binding site for residue EDO C 304 |
| Chain | Residue |
| A | ASN110 |
| A | HOH403 |
| C | ASP229 |
| C | ASP230 |
| site_id | AD6 |
| Number of Residues | 2 |
| Details | binding site for residue EDO C 305 |
| Chain | Residue |
| C | ARG100 |
| C | ASP101 |
| site_id | AD7 |
| Number of Residues | 8 |
| Details | binding site for residue EAJ D 301 |
| Chain | Residue |
| D | ILE102 |
| D | THR209 |
| D | TYR211 |
| D | ARG250 |
| D | HOH401 |
| D | HOH483 |
| D | HOH515 |
| D | HOH631 |
| site_id | AD8 |
| Number of Residues | 5 |
| Details | binding site for residue EDO D 302 |
| Chain | Residue |
| D | TYR177 |
| D | GLU227 |
| D | VAL232 |
| D | HOH443 |
| D | HOH502 |
| site_id | AD9 |
| Number of Residues | 4 |
| Details | binding site for residue EDO D 303 |
| Chain | Residue |
| D | ASP229 |
| D | ASP230 |
| D | HOH413 |
| D | HOH416 |
| site_id | AE1 |
| Number of Residues | 2 |
| Details | binding site for residue EDO D 304 |
| Chain | Residue |
| D | ASN110 |
| D | HOH611 |
| site_id | AE2 |
| Number of Residues | 5 |
| Details | binding site for residue EDO D 305 |
| Chain | Residue |
| D | THR167 |
| D | ILE170 |
| D | SER171 |
| D | HOH455 |
| D | TRP47 |
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 |






