Structure of PDB 5g1a Chain A

Receptor sequence
>5g1aA (length=369) Species: 507 (Alcaligenes) [Search protein sequence]
HHAIGYVWNTLYGWVDTGTGSLAAANLTARMQPISHHLAHPDTKRRFHEL
VCASGQIEHLTPIAAVAATDADILRAHSAAHLENMKRVSNLPTGGDTGDG
ITMMGNGGLEIARLSAGGAVELTRRVATGELSAGYALVNPPGHHAPHNAA
MGFCIFNNTSVAAGYARAVLGMERVAILDWDVHHGNGTQDIWWNDPSVLT
ISLHQHLCFPPDSGYSTERGAGNGHGYNINVPLPPGSGNAAYLHAMDQVV
LPALRAYRPQLIIVGSGFDASMLDPLARMMVTADGFRQMARRTIDCAADI
CDGRIVFVQEGGYSPHYLPFCGLAVIEELTGVRSLPDPYHEFLAGMGGNT
LLDAERAAIEIVPLLADIR
3D structure
PDB5g1a 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
Resolution1.42 Å
3D
structure
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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 D181 H183 D269
BS02 7H1 A L21 I100 H142 H143 G151 F152 D180 H182 F208 Y312 L22 I101 H143 H144 G152 F153 D181 H183 F209 Y313 MOAD: Kd=0.27uM
PDBbind-CN: -logKd/Ki=6.57,Kd=0.27uM
BindingDB: Kd=540nM
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:5g1a, PDBe:5g1a, PDBj:5g1a
PDBsum5g1a
PubMed28389333
UniProtQ70I53|HDAH_ALCSD Histone deacetylase-like amidohydrolase (Gene Name=hdaH)

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