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BioLiP

Structure of PDB 1zz1 Chain D Binding Site BS01

Receptor Information
>1zz1 Chain D (length=367) Species: 242601 (Alcaligenaceae bacterium FB188) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
AIGYVWNTLYGWVDTGTGSLAAANLTARMQPISHHLAHPDTKRRFHELVC
ASGQIEHLTPIAAVAATDADILRAHSAAHLENMKRVSNLPTGGDTGDGIT
MMGNGGLEIARLSAGGAVELTRRVATGELSAGYALVNPPGHHAPHNAAMG
FCIFNNTSVAAGYARAVLGMERVAILDWDVHHGNGTQDIWWNDPSVLTIS
LHQHLCFPPDSGYSTERGAGNGHGYNINVPLPPGSGNAAYLHAMDQVVLP
ALRAYRPQLIIVGSGFDASMLDPLARMMVTADGFRQMARRTIDCAADICD
GRIVFVQEGGYSPHYLPFCGLAVIEELTGVRSLPDPYHEFLAGMGGNTLL
DAERAAIEEIVPLLADI
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 chain1zz1 Chain D Residue 2751 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB1zz1 Crystal structure of a bacterial class 2 histone deacetylase homologue
Resolution1.57 Å
Binding residue
(original residue number in PDB)		D180 H182 D268
Binding residue
(residue number reindexed from 1)		D179 H181 D267
Annotation score1
Enzymatic activity
Enzyme Commision number 3.5.1.-
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:1zz1, PDBe:1zz1, PDBj:1zz1
PDBsum1zz1
PubMed16242151
UniProtQ70I53|HDAH_ALCSD Histone deacetylase-like amidohydrolase (Gene Name=hdaH)

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