Structure of PDB 2bfk Chain A

Receptor sequence
>2bfkA (length=220) Species: 1396 (Bacillus cereus) [Search protein sequence]
TVIKNETGTISISQLNKNVWVHTELGSFNEAVPSNGLVLNTSKGLVLVDS
SWDDKLTKELIEMVEKKFQKRVTDVIITHAHADCIGGIKTLKERGIKAHS
TALTAELAKKNGYEEPLGDLQTVTNLKFGNMKVETFYPGKGHTEDNIVVW
LPQYNILVGGCLVKSTSAKDLGNVADAYVNEWSTSIENVLKRYRNINAVV
PGHGEVGDKGLLLHTLDLLK
3D structure
PDB2bfk Effect of Ph on the Active Site of an Arg121Cys Mutant of the Metallo-Beta-Lactamase from Bacillus Cereus: Implications for the Enzyme Mechanism
ChainA
Resolution2.0 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) H79 H81 D83 H142 C161 K164 N173 H203
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 H79 H81 H142
BS02 ZN A D120 C221 H263 D83 C161 H203
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:2bfk, PDBe:2bfk, PDBj:2bfk
PDBsum2bfk
PubMed15779910
UniProtP04190|BLA2_BACCE Metallo-beta-lactamase type 2 (Gene Name=blm)

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