Structure of PDB 2vun Chain D

Receptor sequence
>2vunD (length=385) Species: 1528 (Eubacterium barkeri) [Search protein sequence]
SKTIIKNIGKIVSGDIKSPVLQADTIVVEDGLIAAIGGEELMKDAGDATI
IDAAGSTVTPGLLDTHVHVSGGDYAPRQKTMDFISSALHGGVTTMISAGS
PHFPGRPKDAAGTKALAITLSKSYYNARPAGVKVHGGAVILEKGLTEEDF
IEMKKEGVWIVGEVGLGTIKNPEDAAPMVEWAHKHGFKVQMHTGGTSIPG
SSTVTADDVIKTKPDVVSHINGGPTAISVQEVDRIMDETDFAMEIVQCGN
PKIADYVARRAAEKGQLGRVIFGNDAPSGTGLIPLGILRNMCQIASMSDI
DPEVAVCMATGNSTAVYGLNTGVIAPGKEADLIIMDTPLGSVAEDAMGAI
AAGDIPGISVVLIDGEAVVTKSRNTPPAKRAAKIL
3D structure
PDB2vun The Crystal Structure of Enamidase: A Bifunctional Enzyme of the Nicotinate Catabolism.
ChainD
Resolution1.89 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 3.5.2.18: enamidase.
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 D H67 H69 E164 D276 H66 H68 E163 D275
BS02 FE D E164 H193 H220 E163 H192 H219
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
View graph for
Biological Process
External links
PDB RCSB:2vun, PDBe:2vun, PDBj:2vun
PDBsum2vun
PubMed18805424
UniProtQ0QLE9|ENA_EUBBA Enamidase (Gene Name=Ena)

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