Structure of PDB 4c1h Chain A

Receptor sequence
>4c1hA (length=221) Species: 1396 (Bacillus cereus) [Search protein sequence]
TVIKNETGTISISQLNKNVWVHTELGSFNGEAVPSNGLVLNTSKGLVLVD
SSWDDKLTKELIEMVEKKFQKRVTDVIITHAHADRIGGIKTLKERGIKAH
STALTAELAKKNGYEEPLGDLQTVTNLKFGNMKVETFYPGKGHTEDNIVV
WLPQYNILVGGCLVKSTSAKDLGNVADAYVNEWSTSIENVLKRYRNINAV
VPGHGEVGDKGLLLHTLDLLK
3D structure
PDB4c1h Structural Basis of Metallo-beta-Lactamase Inhibition by Captopril Stereoisomers.
ChainA
Resolution1.1 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H116 H118 D120 H179 C198 K201 N210 H240
Catalytic site (residue number reindexed from 1) H80 H82 D84 H143 C162 K165 N174 H204
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 X8Z A W89 H118 D120 H179 C198 G209 N210 H240 W53 H82 D84 H143 C162 G173 N174 H204 PDBbind-CN: -logKd/Ki=4.09,IC50=80.4uM
BS02 ZN A D120 C198 H240 D84 C162 H204
BS03 ZN A H116 H118 H179 H80 H82 H143
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:4c1h, PDBe:4c1h, PDBj:4c1h
PDBsum4c1h
PubMed26482303
UniProtP04190|BLA2_BACCE Metallo-beta-lactamase type 2 (Gene Name=blm)

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