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

5QAU

OXA-48 IN COMPLEX WITH COMPOUND 26a

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
B0008658molecular_functionpenicillin binding
B0008800molecular_functionbeta-lactamase activity
B0016787molecular_functionhydrolase activity
B0017001biological_processantibiotic catabolic process
B0046677biological_processresponse to antibiotic
B0046872molecular_functionmetal ion binding
C0008658molecular_functionpenicillin binding
C0008800molecular_functionbeta-lactamase activity
C0016787molecular_functionhydrolase activity
C0017001biological_processantibiotic catabolic process
C0046677biological_processresponse to antibiotic
C0046872molecular_functionmetal ion binding
D0008658molecular_functionpenicillin binding
D0008800molecular_functionbeta-lactamase activity
D0016787molecular_functionhydrolase activity
D0017001biological_processantibiotic catabolic process
D0046677biological_processresponse to antibiotic
D0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues2
Detailsbinding site for residue CL A 301
ChainResidue
AARG206
CARG206

site_idAC2
Number of Residues5
Detailsbinding site for residue EDO A 302
ChainResidue
ALYS94
ATRP95
AASP96
AHOH452
AHOH462

site_idAC3
Number of Residues7
Detailsbinding site for residue EDO A 303
ChainResidue
AHOH426
AHOH428
AHOH522
CASP88
CHIS90
AHIS178
AASN179

site_idAC4
Number of Residues5
Detailsbinding site for residue EDO A 304
ChainResidue
AGLN64
AALA65
APRO217
AHOH483
AHOH554

site_idAC5
Number of Residues5
Detailsbinding site for residue EDO B 301
ChainResidue
AARG214
BARG100
BHOH416
BHOH471
BHOH549

site_idAC6
Number of Residues4
Detailsbinding site for residue EDO B 302
ChainResidue
BASN110
BHOH403
BHOH526
BHOH538

site_idAC7
Number of Residues7
Detailsbinding site for residue V7V C 301
ChainResidue
CSER70
CSER118
CTHR209
CGLY210
CTYR211
CARG250
CHOH401

site_idAC8
Number of Residues7
Detailsbinding site for residue EDO C 302
ChainResidue
AHIS90
AHOH412
CTYR177
CGLU227
CVAL232
CHOH423
CHOH482

site_idAC9
Number of Residues4
Detailsbinding site for residue EDO C 303
ChainResidue
BLYS60
BGLN64
CASN146
CGLU147

site_idAD1
Number of Residues9
Detailsbinding site for residue V7V D 301
ChainResidue
DSER70
DSER118
DTHR209
DGLY210
DTYR211
DSER244
DLEU247
DARG250
DHOH401

site_idAD2
Number of Residues1
Detailsbinding site for residue CL D 302
ChainResidue
DARG206

site_idAD3
Number of Residues4
Detailsbinding site for residue EDO D 303
ChainResidue
DLYS94
DTRP95
DASP96
DHOH432

site_idAD4
Number of Residues9
Detailsbinding site for residue EDO D 304
ChainResidue
DMET115
DALA194
DMET195
DLEU196
DTHR197
DALA207
DLYS208
DHOH415
DHOH425

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

222926

PDB entries from 2024-07-24

PDB statisticsPDBj update infoContact PDBjnumon