Structure of PDB 4cog Chain B Binding Site BS02

Receptor Information
>4cog Chain B (length=207) Species: 216591 (Burkholderia cenocepacia J2315) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
TLWDISPPVSPATPVWPGDTPVAVERVWRMEAGSPVNVARLTLSPHTGAH
CDAPLHYDADGAPIGAVPLDTYLGPCRVIHCIGAAPVVRPADVEAALDGV
PPRVLLRTYARAAVEQWDSNFCAVAPDTVDLLAAHGVKLIGIDTPSLDPQ
ESKTMDAHRRVRAHRMAILEGIVLDDVPPGDYELIALPLKFATLDASPVR
AVLRALP
Ligand information
Ligand IDMG
InChIInChI=1S/Mg/q+2
InChIKeyJLVVSXFLKOJNIY-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0
[Mg+2]
CACTVS 3.341[Mg++]
FormulaMg
NameMAGNESIUM ION
ChEMBL
DrugBankDB01378
ZINC
PDB chain4cog Chain B Residue 1210 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB4cog Structure of Bacterial Kynurenine Formamidase Reveals a Crowded Binuclear-Zinc Catalytic Site Primed to Generate a Potent Nucleophile.
Resolution1.6 Å
Binding residue
(original residue number in PDB)
D60 D62
Binding residue
(residue number reindexed from 1)
D58 D60
Annotation score1
Enzymatic activity
Enzyme Commision number 3.5.1.9: arylformamidase.
Gene Ontology
Molecular Function
GO:0004061 arylformamidase activity
GO:0004328 formamidase activity
GO:0008270 zinc ion binding
GO:0016787 hydrolase activity
GO:0046872 metal ion binding
Biological Process
GO:0006569 tryptophan catabolic process
GO:0019441 tryptophan catabolic process to kynurenine
GO:0043420 anthranilate metabolic process

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Molecular Function

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Biological Process
External links
PDB RCSB:4cog, PDBe:4cog, PDBj:4cog
PDBsum4cog
PubMed24942958
UniProtB4E9I9|KYNB_BURCJ Kynurenine formamidase (Gene Name=kynB)

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