Structure of PDB 1bc2 Chain B

Receptor sequence
>1bc2B (length=216) Species: 1396 (Bacillus cereus) [Search protein sequence]
TVIKNETGTISISQLNKNVWVHTELGAVPSNGLVLNTSKGLVLVDSSWDD
KLTKELIEMVEKKFQKRVTDVIITHAHADRIGGIKTLKERGIKAHSTALT
AELAKKNGYEEPLGDLQTVTNLKFGNMKVETFYPGKGHTEDNIVVWLPQY
NILVGGCLVKSTSAKDLGNVADAYVNEWSTSIENVLKRYRNINAVVPGHG
EVGDKGLLLHTLDLLK
3D structure
PDB1bc2 Crystal structure of the zinc-dependent beta-lactamase from Bacillus cereus at 1.9 A resolution: binuclear active site with features of a mononuclear enzyme.
ChainB
Resolution1.9 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) H75 H77 D79 H138 C157 K160 N169 H199
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 B H86 H88 H149 H75 H77 H138
BS02 ZN B C168 H210 C157 H199
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:1bc2, PDBe:1bc2, PDBj:1bc2
PDBsum1bc2
PubMed9730812
UniProtP04190|BLA2_BACCE Metallo-beta-lactamase type 2 (Gene Name=blm)

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