Structure of PDB 4nq6 Chain A

Receptor sequence
>4nq6A (length=222) Species: 1396 (Bacillus cereus) [Search protein sequence]
KTVIKNETGTISISQLNKNVWVHTELGSFNGEAVPSNGLVLNTSKGLVLV
DSSWDDKLTKELIEMVEKKFQKRVTDVIITHAHADRIGGIKTLKERGIKA
HSTALTAELAKKNGYEEPLGDLQTVTNLKFGNMKVETFYPGKGHTEDNIV
VWLPQYNILVGGCLVKSTSAKDLGNVADAYVNEWSTSIENVLKRYRNINA
VVPGHGEVGDKGLLLHTLDLLK
3D structure
PDB4nq6 Cross-class metallo-beta-lactamase inhibition by bisthiazolidines reveals multiple binding modes.
ChainA
Resolution1.8 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H86 H88 D90 H149 C168 K171 N180 H210
Catalytic site (residue number reindexed from 1) H81 H83 D85 H144 C163 K166 N175 H205
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 ZN A H86 H88 H149 H81 H83 H144
BS02 ZN A C168 H210 C163 H205
BS03 3R9 A F34 W59 H88 D90 H149 C168 H210 F29 W54 H83 D85 H144 C163 H205 PDBbind-CN: -logKd/Ki=4.28,Ki=53uM
Gene Ontology
Molecular Function
GO:0008270 zinc ion binding
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:0042597 periplasmic space

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Cellular Component
External links
PDB RCSB:4nq6, PDBe:4nq6, PDBj:4nq6
PDBsum4nq6
PubMed27303030
UniProtP04190|BLA2_BACCE Metallo-beta-lactamase type 2 (Gene Name=blm)

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