Structure of PDB 3knr Chain B

Receptor sequence
>3knrB (length=205) Species: 1396 (Bacillus cereus) [Search protein sequence]
TISISQLNKNVWVHTELPSNGLVLNTSKGLVLVDSSWDDKLTKELIEMVE
KKFQKRVTDVIITHAHADRIGGIKTLKERGIKAHSTALTAELAKKNGYEE
PLGDLQTVTNLKFGNMKVETFYPGKGHTEDNIVVWLPQYNILVGGDLVKS
TSAKDLGNVADAYVNEWSTSIENVLKRYRNINAVVPGHGEVGDKGLLLHT
LDLLK
3D structure
PDB3knr Metallo-beta-lactamases withstand low Zn(II) conditions by tuning metal-ligand interactions.
ChainB
Resolution1.71 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 D168 K171 N180 H210
Catalytic site (residue number reindexed from 1) H64 H66 D68 H127 D146 K149 N158 H188
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 H64 H66 H127
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:3knr, PDBe:3knr, PDBj:3knr
PDBsum3knr
PubMed22729148
UniProtP04190|BLA2_BACCE Metallo-beta-lactamase type 2 (Gene Name=blm)

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