Structure of PDB 1zz0 Chain D Binding Site BS02
Receptor Information
>1zz0 Chain D (length=367) Species:
242601
(Alcaligenaceae bacterium FB188) [
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AIGYVWNTLYGWVDTGTGSLAAANLTARMQPISHHLAHPDTKRRFHELVC
ASGQIEHLTPIAAVAATDADILRAHSAAHLENMKRVSNLPTGGDTGDGIT
MMGNGGLEIARLSAGGAVELTRRVATGELSAGYALVNPPGHHAPHNAAMG
FCIFNNTSVAAGYARAVLGMERVAILDWDVHHGNGTQDIWWNDPSVLTIS
LHQHLCFPPDSGYSTERGAGNGHGYNINVPLPPGSGNAAYLHAMDQVVLP
ALRAYRPQLIIVGSGFDASMLDPLARMMVTADGFRQMARRTIDCAADICD
GRIVFVQEGGYSPHYLPFCGLAVIEELTGVRSLPDPYHEFLAGMGGNTLL
DAERAAIEEIVPLLADI
Ligand information
Ligand ID
ACT
InChI
InChI=1S/C2H4O2/c1-2(3)4/h1H3,(H,3,4)/p-1
InChIKey
QTBSBXVTEAMEQO-UHFFFAOYSA-M
SMILES
Software
SMILES
ACDLabs 10.04
[O-]C(=O)C
OpenEye OEToolkits 1.5.0
CC(=O)[O-]
CACTVS 3.341
CC([O-])=O
Formula
C2 H3 O2
Name
ACETATE ION
ChEMBL
DrugBank
DB14511
ZINC
PDB chain
1zz0 Chain D Residue 1752 [
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Receptor-Ligand Complex Structure
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PDB
1zz0
Crystal structure of a bacterial class 2 histone deacetylase homologue
Resolution
1.6 Å
Binding residue
(original residue number in PDB)
H142 H143 D180 H182 Y312
Binding residue
(residue number reindexed from 1)
H141 H142 D179 H181 Y311
Annotation score
5
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:1zz0
,
PDBe:1zz0
,
PDBj:1zz0
PDBsum
1zz0
PubMed
16242151
UniProt
Q70I53
|HDAH_ALCSD Histone deacetylase-like amidohydrolase (Gene Name=hdaH)
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