Structure of PDB 5g17 Chain A

Receptor sequence
>5g17A (length=368) Species: 507 (Alcaligenes) [Search protein sequence]
AIGYVWNTLYGWVDTGTGSLAAANLTARMQPISHHLAHPDTKRRFHELVC
ASGQIEHLTPIAAVAATDADILRAHSAAHLENMKRVSNLPTGGDTGDGIA
MMGNGGLEIARLSAGGAVELTRRVATGELSAGYALVNPPGHHAPHNAAMG
FCIFNNTSVAAGYARAVLGMERVAILDWDVHHGNGTQDIWWNDPSVLTIS
LHQHLCFPPDSGYSTERGAGNGHGYNINVPLPPGSGNAAYLHAMDQVVLP
ALRAYRPQLIIVGSGFDASMLDPLARMMVTADGFRQMARRTIDCAADICD
GRIVFVQEGGYSPHYLPFCGLAVIEELTGVRSLPDPYHEFLAGMGGNTLL
DAERAAIEEIVPLLADIR
3D structure
PDB5g17 The thermodynamic signature of ligand binding to histone deacetylase-like amidohydrolases is most sensitive to the flexibility in the L2-loop lining the active site pocket.
ChainA
Resolution1.51 Å
3D
structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
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 ZN A D180 H182 D268 D179 H181 D267
BS02 6DK A P140 H142 H143 G151 F152 D180 H182 F208 G310 Y312 P139 H141 H142 G150 F151 D179 H181 F207 G309 Y311 MOAD: Kd=0.2uM
PDBbind-CN: -logKd/Ki=6.70,Kd=0.2uM
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

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:5g17, PDBe:5g17, PDBj:5g17
PDBsum5g17
PubMed28389333
UniProtQ70I53|HDAH_ALCSD Histone deacetylase-like amidohydrolase (Gene Name=hdaH)

[Back to BioLiP]