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BioLiP

Structure of PDB 3i14 Chain A Binding Site BS02

Receptor Information
>3i14 Chain A (length=215) Species: 1396 (Bacillus cereus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
KTVIKNETGTISISQLNKNVWVHTELVPSNGLVLNTSKGLVLVDSSWDDK
LTKELIEMVEKKFQKRVTDVIITHAHADRIGGIKTLKERGIKAHSTALTA
ELAKKNGYEEPLGDLQTVTNLKFGNMKVETFYPGKGHTEDNIVVWLPQYN
ILVGGCLVKSTSAKDLGNVADAYVNEWSTSIENVLKRYRNINAVVPGHGE
VGDKGLLLHTLDLLK
Ligand information
Ligand IDCO
InChIInChI=1S/Co/q+2
InChIKeyXLJKHNWPARRRJB-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0		[Co+2]
CACTVS 3.341[Co++]
FormulaCo
NameCOBALT (II) ION
ChEMBL
DrugBankDB14205
ZINC
PDB chain3i14 Chain A Residue 229 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB3i14 Evidence of adaptability in metal coordination geometry and active-site loop conformation among B1 metallo-beta-lactamases .
Resolution1.55 Å
Binding residue
(original residue number in PDB)		D90 C168 H210
Binding residue
(residue number reindexed from 1)		D78 C156 H198
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) H86 H88 D90 H149 C168 K171 N180 H210
Catalytic site (residue number reindexed from 1) H74 H76 D78 H137 C156 K159 N168 H198
Enzyme Commision number 3.5.2.6: beta-lactamase.
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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Biological Process
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Cellular Component
External links
PDB RCSB:3i14, PDBe:3i14, PDBj:3i14
PDBsum3i14
PubMed20677753
UniProtP04190|BLA2_BACCE Metallo-beta-lactamase type 2 (Gene Name=blm)

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