Structure of PDB 3knr Chain A

Receptor sequence
>3knrA (length=214) Species: 1396 (Bacillus cereus) [Search protein sequence]
GTISISQLNKNVWVHTELGSFNGEAVPSNGLVLNTSKGLVLVDSSWDDKL
TKELIEMVEKKFQKRVTDVIITHAHADRIGGIKTLKERGIKAHSTALTAE
LAKKNGYEEPLGDLQTVTNLKFGNMKVETFYPGKGHTEDNIVVWLPQYNI
LVGGDLVKSTSAKDLGNVADAYVNEWSTSIENVLKRYRNINAVVPGHGEV
GDKGLLLHTLDLLK
3D structure
PDB3knr Metallo-beta-lactamases withstand low Zn(II) conditions by tuning metal-ligand interactions.
ChainA
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) H73 H75 D77 H136 D155 K158 N167 H197
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 H86 H88 H149 H73 H75 H136
BS02 ZN A D90 D168 H210 D77 D155 H197
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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