Structure of PDB 4nq5 Chain A

Receptor sequence
>4nq5A (length=215) Species: 1396 (Bacillus cereus) [Search protein sequence]
TVIKNETGTISISQLNKNVWVHTELAVPSNGLVLNTSKGLVLVDSSWDDK
LTKELIEMVEKKFQKRVTDVIITHAHADRIGGIKTLKERGIKAHSTALTA
ELAKKNGYEEPLGDLQTVTNLKFGNMKVETFYPGKGHTEDNIVVWLPQYN
ILVGGCLVKSTSAKDLGNVADAYVNEWSTSIENVLKRYRNINAVVPGHGE
VGDKGLLLHTLDLLK
3D structure
PDB4nq5 Inhibition of metallo-lactamases with bicyclic compounds
ChainA
Resolution2.29 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) H74 H76 D78 H137 C156 K159 N168 H198
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 H74 H76 H137
BS02 ZN A D90 C168 H210 D78 C156 H198
BS03 3C7 A W59 H88 D90 H149 G179 N180 H210 W47 H76 D78 H137 G167 N168 H198
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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Biological Process
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Cellular Component
External links
PDB RCSB:4nq5, PDBe:4nq5, PDBj:4nq5
PDBsum4nq5
PubMed
UniProtP04190|BLA2_BACCE Metallo-beta-lactamase type 2 (Gene Name=blm)

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