Structure of PDB 3men Chain C Binding Site BS01

Receptor Information
>3men Chain C (length=337) Species: 320372 (Burkholderia pseudomallei 1710b) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
SMLTYFHPDQSLHHPRTYFSRGRMRMPQEVPERAARLVAAAFAMGFPVRE
PDDFGIAPIAAVHDTHYLRFLETVHREWKAMPEDWGDEAMSNIFVREPNA
LRGVLAQAARHLADGSCPVGEHTWRAAYWSAQSALAAAAAVRDGAPAAYA
LCRPPGHHARVDAAGGFCYLNNAAIAAQALRARHARVAVLDTDMHHGQGI
QEIFYARRDVLYVSIHGDPTNFYPAVAGFDDERGAGEGLGYNVNLPMPHG
SSEAAFFERVDDALRELRRFAPDALVLSLGFDVYRDDPQSQVAVTTDGFG
RLGHLIGALRLPTVIVQEGGYHIESLEANARSFFGGF
Ligand information
Ligand IDZN
InChIInChI=1S/Zn/q+2
InChIKeyPTFCDOFLOPIGGS-UHFFFAOYSA-N
SMILES
SoftwareSMILES
CACTVS 3.341[Zn++]
ACDLabs 10.04
OpenEye OEToolkits 1.5.0		[Zn+2]
FormulaZn
NameZINC ION
ChEMBLCHEMBL1236970
DrugBankDB14532
ZINC
PDB chain3men Chain C Residue 400 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB3men SAD phasing using iodide ions in a high-throughput structural genomics environment.
Resolution2.2 Å
Binding residue
(original residue number in PDB)		D192 H194 D281
Binding residue
(residue number reindexed from 1)		D193 H195 D282
Annotation score1
Enzymatic activity
Enzyme Commision number 3.5.1.-
3.5.1.62: acetylputrescine deacetylase.
Gene Ontology
Molecular Function
GO:0004407 histone deacetylase activity
GO:0016787 hydrolase activity
GO:0046872 metal ion binding
GO:0047609 acetylputrescine deacetylase activity
Biological Process
GO:0006338 chromatin remodeling

View graph for
Molecular Function
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Biological Process
External links
PDB RCSB:3men, PDBe:3men, PDBj:3men
PDBsum3men
PubMed21359836
UniProtQ3JUN4|APAHL_BURP1 Acetylpolyamine amidohydrolase (Gene Name=aphA)

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