Structure of PDB 2vcg Chain D

Receptor sequence
>2vcgD (length=375) Species: 512 (Alcaligenes sp.) [Search protein sequence]
MHHHHHHAIGYVWNTLYGWVDTGTGSLAAANLTARMQPISHHLAHPDTKR
RFHELVCASGQIEHLTPIAAVAATDADILRAHSAAHLENMKRVSNLPTGG
DTGDGITMMGNGGLEIARLSAGGAVELTRRVATGELSAGYALVNPPGHHA
PHNAAMGFCIFNNTSVAAGYARAVLGMERVAILDWDVHHGNGTQDIWWND
PSVLTISLHQHLCFPPDSGYSTERGAGNGHGYNINVPLPPGSGNAAYLHA
MDQVVLPALRAYRPQLIIVGSGFDASMLDPLARMMVTADGFRQMARRTID
CAADICDGRIVFVQEGGYSPHYLPFCGLAVIEELTGVRSLPDPYHEFLAG
MGGNTLLDAERAAIEEIVPLLADIR
3D structure
PDB2vcg Phenylalanine-Containing Hydroxamic Acids as Selective Inhibitors of Class Iib Histone Deacetylases (Hdacs).
ChainD
Resolution1.9 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 3.5.1.-
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 S17 D E346 F347 E346 F347 PDBbind-CN: -logKd/Ki=5.77,IC50=1.69uM
BS02 ZN D D186 H188 D274 D186 H188 D274
BS03 ZN D H4 H6 H64 H4 H6 H64
BS04 S17 D L27 I106 H148 H149 F158 D186 H188 F214 Y318 L27 I106 H148 H149 F158 D186 H188 F214 Y318 PDBbind-CN: -logKd/Ki=5.77,IC50=1.69uM
Gene Ontology
Molecular Function
GO:0004407 histone deacetylase activity
GO:0016787 hydrolase activity
GO:0046872 metal ion binding
Biological Process
GO:0000122 negative regulation of transcription by RNA polymerase II
GO:0006338 chromatin remodeling

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Molecular Function
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Biological Process
External links
PDB RCSB:2vcg, PDBe:2vcg, PDBj:2vcg
PDBsum2vcg
PubMed18054239
UniProtQ70I53|HDAH_ALCSD Histone deacetylase-like amidohydrolase (Gene Name=hdaH)

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