Structure of PDB 2vun Chain D Binding Site BS02

Receptor Information

>2vun Chain D (length=385) Species: 1528 (Eubacterium barkeri) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]

SKTIIKNIGKIVSGDIKSPVLQADTIVVEDGLIAAIGGEELMKDAGDATI
IDAAGSTVTPGLLDTHVHVSGGDYAPRQKTMDFISSALHGGVTTMISAGS
PHFPGRPKDAAGTKALAITLSKSYYNARPAGVKVHGGAVILEKGLTEEDF
IEMKKEGVWIVGEVGLGTIKNPEDAAPMVEWAHKHGFKVQMHTGGTSIPG
SSTVTADDVIKTKPDVVSHINGGPTAISVQEVDRIMDETDFAMEIVQCGN
PKIADYVARRAAEKGQLGRVIFGNDAPSGTGLIPLGILRNMCQIASMSDI
DPEVAVCMATGNSTAVYGLNTGVIAPGKEADLIIMDTPLGSVAEDAMGAI
AAGDIPGISVVLIDGEAVVTKSRNTPPAKRAAKIL

Ligand information

Ligand ID

InChI

InChI=1S/Fe/q+3

InChIKey

VTLYFUHAOXGGBS-UHFFFAOYSA-N

SMILES

Software	SMILES
ACDLabs 10.04 CACTVS 3.341 OpenEye OEToolkits 1.5.0	[Fe+3]

Formula

Name

FE (III) ION

PDB chain

2vun Chain D Residue 402 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]

Receptor-Ligand Complex Structure

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Structure summary

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PDB	2vun The Crystal Structure of Enamidase: A Bifunctional Enzyme of the Nicotinate Catabolism.
Resolution	1.89 Å
Binding residue (original residue number in PDB)	E164 H193 H220
Binding residue (residue number reindexed from 1)	E163 H192 H219
Annotation score	1

Enzymatic activity

Enzyme Commision number

3.5.2.18: enamidase.

Gene Ontology

	Molecular Function
GO:0016787	hydrolase activity
GO:0016810	hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
GO:0043792	enamidase activity
GO:0046872	metal ion binding

	Biological Process
GO:1901848	nicotinate catabolic process

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Molecular Function

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Biological Process

External links

PDB	RCSB:2vun, PDBe:2vun, PDBj:2vun
PDBsum	2vun
PubMed	18805424
UniProt	Q0QLE9\|ENA_EUBBA Enamidase (Gene Name=Ena)

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