Structure of PDB 1c3r Chain A

Receptor sequence
>1c3rA (length=372) Species: 63363 (Aquifex aeolicus) [Search protein sequence]
KKVKLIGTLDYGKYRYPKNHPLKIPRVSLLLRFKDAMNLIDEKELIKSRP
ATKEELLLFHTEDYINTLMEAERSQSVPKGAREKYNIGGYENPVSYAMFT
GSSLATGSTVQAIEEFLKGNVAFNPAGGMHHAFKSRANGFCYINNPAVGI
EYLRKKGFKRILYIDLDAHHCDGVQEAFYDTDQVFVLSLHQSPEYAFPFE
KGFLEEIGEGKGKGYNLNIPLPKGLNDNEFLFALEKSLEIVKEVFEPEVY
LLQLGTDPLLEDYLSKFNLSNVAFLKAFNIVREVFGEGVYLGGGGYHPYA
LARAWTLIWCELSGREVPEKLNNKAKELLKSIDFEEFDDEVDRSYMLETL
KDPWRGGEVRKEVKDTLEKAKA
3D structure
PDB1c3r Structures of a histone deacetylase homologue bound to the TSA and SAHA inhibitors.
ChainA
Resolution2.0 Å
3D
structure
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Enzymatic activity
Enzyme Commision number ?
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 A D168 H170 D258 D167 H169 D257
BS02 TSN A P22 H131 H132 F141 D168 H170 Y297 P21 H130 H131 F140 D167 H169 Y296 PDBbind-CN: -logKd/Ki=6.40,IC50=0.4uM
Gene Ontology
Molecular Function
GO:0004407 histone deacetylase activity
GO:0046872 metal ion binding
Biological Process
GO:0040029 epigenetic regulation of gene expression
GO:0045149 acetoin metabolic process
GO:0045150 acetoin catabolic process

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Molecular Function
View graph for
Biological Process
External links
PDB RCSB:1c3r, PDBe:1c3r, PDBj:1c3r
PDBsum1c3r
PubMed10490031
UniProtO67135

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