Structure of PDB 3fcz Chain A

Receptor sequence
>3fczA (length=219) Species: 1396 (Bacillus cereus) [Search protein sequence]
KTVIKNETGTISISQLNKNVWVHTELGSFAVPSSGLVLNTSKGLVLVDSS
WDDKLTKELIEMVEKKFQKRVTDAIITHAHADRIGGIKTLKERGIKAHST
ALTAELAKKNGYEEPLGDLQTVTNLKFGNMKVETFYPGKGHTEDNIVVWL
PQYNILVGGCLVKSTSAKDLGNVADAYVNEWSTSIENVSKRYRNINAVVP
SHGEVGDKGLLLHTLDLLK
3D structure
PDB3fcz Adaptive protein evolution grants organismal fitness by improving catalysis and flexibility.
ChainA
Resolution2.804 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 H196 C221 K224 N233 H263
Catalytic site (residue number reindexed from 1) H78 H80 D82 H141 C160 K163 N172 H202
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 H116 H118 H196 H78 H80 H141
BS02 ZN A D120 C221 H263 D82 C160 H202
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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Molecular Function
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Cellular Component
External links
PDB RCSB:3fcz, PDBe:3fcz, PDBj:3fcz
PDBsum3fcz
PubMed19098096
UniProtP04190|BLA2_BACCE Metallo-beta-lactamase type 2 (Gene Name=blm)

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