Structure of PDB 4wbg Chain A

Receptor sequence
>4wbgA (length=347) Species: 573 (Klebsiella pneumoniae) [Search protein sequence]
DPLRPVVDASIQPLLKEHRIPGMAVAVLKDGKAHYFNYGVANRESGASVS
EQTLFEIGSVSKTLTATLGAYAVVKGAMQLDDKASRHAPWLKGSVFDSIT
MGELATYSAGGLPLQFPEEVDSSEKMRAYYRQWAPVYSPGSHRQYSNPSI
GLFGHLAASSLKQPFAQLMEQTLLPGLGMHHTYVNVPKQAMASYAYGYSK
EDKPIRVGMLADEAYGIKTSSADLLAFVKANIGGVDDKALQQAISLTHKG
HYSVGGMTQGLGWESYAYPVTEQTLLAGNSAKVILEANPTAAPRQVLFNK
TGSSNGFGAYVAFVPARGIGIVMLANRNYPIPARVKAAHAILAQLAG
3D structure
PDB4wbg Conformational Change Observed in the Active Site of Class C beta-Lactamase MOX-1 upon Binding to Aztreonam
ChainA
Resolution1.9 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) S65 K68 M107 E109 F122 Y151 G157 E272 K312 S315
Catalytic site (residue number reindexed from 1) S59 K62 M101 E103 F116 Y145 G151 E264 K300 S303
Enzyme Commision number 3.5.2.6: beta-lactamase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 AZR A S65 Q121 Y151 Y223 I292 T313 G314 S315 S59 Q115 Y145 Y215 I284 T301 G302 S303 PDBbind-CN: -logKd/Ki=5.55,Ki=2.85uM
Gene Ontology
Molecular Function
GO:0008800 beta-lactamase activity
GO:0016787 hydrolase activity
GO:0046872 metal ion binding
Biological Process
GO:0017001 antibiotic catabolic process
GO:0046677 response to antibiotic
Cellular Component
GO:0030288 outer membrane-bounded periplasmic space

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:4wbg, PDBe:4wbg, PDBj:4wbg
PDBsum4wbg
PubMed26055361
UniProtQ51578

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