Structure of PDB 3q9b Chain G

Receptor sequence
>3q9bG (length=341) Species: 40837 (Mycoplana ramosa) [Search protein sequence]
MRVIFSEDHKLRNAKTELYGGELVPPFEAPFRAEWILAAVKEAGFDDVVA
PARHGLETVLKVHDAGYLNFLETAWDRWKAAGYKGEAIATSFPVRRTSPR
IPTDIEGQIGYYCNAAETAISPGTWEAALSSMASAIDGADLIAAGHKAAF
SLCRPPGHHAGIDMFGGYCFINNAAVAAQRLLDKGAKKIAILDVDFHHGN
GTQDIFYERGDVFFASLHGDPAEAFPHFLGYAEETGKGAGAGTTANYPMG
RGTPYSVWGEALTDSLKRIAAFGAEAIVVSLGVDTFEQDPISFFKLTSPD
YITMGRTIAASGVPLLVVMEGGYGVPEIGLNVANVLKGVAG
3D structure
PDB3q9b Structure of prokaryotic polyamine deacetylase reveals evolutionary functional relationships with eukaryotic histone deacetylases .
ChainG
Resolution2.25 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 3.5.1.-
3.5.1.48: acetylspermidine deacetylase.
3.5.1.62: acetylputrescine deacetylase.
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 B3N G Y19 F27 H158 H159 Y168 D195 H197 F225 P290 I291 Y19 F27 H158 H159 Y168 D195 H197 F225 P290 I291
BS02 ZN G D195 H197 D284 D195 H197 D284
Gene Ontology
Molecular Function
GO:0004407 histone deacetylase activity
GO:0016787 hydrolase activity
GO:0046872 metal ion binding
GO:0047609 acetylputrescine deacetylase activity
GO:0047611 acetylspermidine deacetylase activity
Biological Process
GO:0006338 chromatin remodeling

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Molecular Function
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Biological Process
External links
PDB RCSB:3q9b, PDBe:3q9b, PDBj:3q9b
PDBsum3q9b
PubMed21268586
UniProtQ48935|APAH_MYCRA Acetylpolyamine amidohydrolase (Gene Name=aphA)

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