Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

5QB1

OXA-48 IN COMPLEX WITH COMPOUND 36

Functional Information from GO Data
ChainGOidnamespacecontents
A0008658molecular_functionpenicillin binding
A0008800molecular_functionbeta-lactamase activity
A0016787molecular_functionhydrolase activity
A0017001biological_processantibiotic catabolic process
A0046677biological_processresponse to antibiotic
A0046872molecular_functionmetal ion binding
A0071555biological_processcell wall organization
B0008658molecular_functionpenicillin binding
B0008800molecular_functionbeta-lactamase activity
B0016787molecular_functionhydrolase activity
B0017001biological_processantibiotic catabolic process
B0046677biological_processresponse to antibiotic
B0046872molecular_functionmetal ion binding
B0071555biological_processcell wall organization
C0008658molecular_functionpenicillin binding
C0008800molecular_functionbeta-lactamase activity
C0016787molecular_functionhydrolase activity
C0017001biological_processantibiotic catabolic process
C0046677biological_processresponse to antibiotic
C0046872molecular_functionmetal ion binding
C0071555biological_processcell wall organization
D0008658molecular_functionpenicillin binding
D0008800molecular_functionbeta-lactamase activity
D0016787molecular_functionhydrolase activity
D0017001biological_processantibiotic catabolic process
D0046677biological_processresponse to antibiotic
D0046872molecular_functionmetal ion binding
D0071555biological_processcell wall organization
Functional Information from PDB Data
site_idAC1
Number of Residues2
Detailsbinding site for residue CL A 301
ChainResidue
AARG206
DARG206

site_idAC2
Number of Residues5
Detailsbinding site for residue EDO A 302
ChainResidue
ALEU81
ASER184
AARG186
ASER187
AHOH404

site_idAC3
Number of Residues7
Detailsbinding site for residue EDO A 303
ChainResidue
AVAL232
AHOH406
DHIS90
DGLN193
DHOH440
ATYR177
AGLU227

site_idAC4
Number of Residues9
Detailsbinding site for residue F1C B 301
ChainResidue
BSER70
BVAL120
BTHR209
BTHR213
BARG214
BSER244
BLEU247
BARG250
BHOH437

site_idAC5
Number of Residues1
Detailsbinding site for residue CL B 302
ChainResidue
BARG206

site_idAC6
Number of Residues1
Detailsbinding site for residue EDO B 303
ChainResidue
BLYS116

site_idAC7
Number of Residues5
Detailsbinding site for residue EDO B 304
ChainResidue
BTYR177
BGLU227
BVAL232
BHOH418
BHOH426

site_idAC8
Number of Residues2
Detailsbinding site for residue EDO B 305
ChainResidue
BARG107
BASN110

site_idAC9
Number of Residues3
Detailsbinding site for residue EDO C 301
ChainResidue
CLYS116
CHOH407
CHOH434

site_idAD1
Number of Residues3
Detailsbinding site for residue EDO C 302
ChainResidue
CSER171
CARG174
CHOH437

site_idAD2
Number of Residues9
Detailsbinding site for residue F1C D 301
ChainResidue
DSER70
DVAL120
DTHR209
DTYR211
DARG214
DSER244
DLEU247
DARG250
DHOH401

site_idAD3
Number of Residues5
Detailsbinding site for residue EDO D 302
ChainResidue
AASN200
AASP229
DLYS116
DHOH418
DHOH441

Functional Information from PROSITE/UniProt
site_idPS00337
Number of Residues11
DetailsBETA_LACTAMASE_D Beta-lactamase class-D active site. PaSTFKIPnSL
ChainResidueDetails
APRO68-LEU78

226707

PDB entries from 2024-10-30

PDB statisticsPDBj update infoContact PDBjnumon