Structure of PDB 4zuq Chain A

Receptor sequence
>4zuqA (length=341) Species: 40837 (Mycoplana ramosa) [Search protein sequence]
MRVIFSEDHKLRNAKTELYGGELVPPFEAPFRAEWILAAVKEAGFDDVVA
PARHGLETVLKVHDAGYLNFLETAWDRWKAAGYKGEAIATSFPVRRTSPR
IPTDIEGQIGYYCNAAETAISPGTWEAALSSMASAIDGADLIAAGHKAAF
SLCRPPGHHAGIDMFGGYCFINNAAVAAQRLLDKGAKKIAILDVDFHHGN
GTQDIFYERGDVFFASLHGDPAEAFPHFLGYAEETGKGAGAGTTANYPMG
RGTPYSVWGEALTDSLKRIAAFGAEAIVVSLGVDTFEQDPISFFKLTSPD
YITMGRTIAASGVPLLVVMEGGYGVPEIGLNVANVLKGVAG
3D structure
PDB4zuq Design, Synthesis, and Evaluation of Polyamine Deacetylase Inhibitors, and High-Resolution Crystal Structures of Their Complexes with Acetylpolyamine Amidohydrolase.
ChainA
Resolution1.22 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 6XA A H158 H159 Y168 D195 H197 F225 Y323 H158 H159 Y168 D195 H197 F225 Y323 MOAD: ic50=0.13uM
PDBbind-CN: -logKd/Ki=6.89,IC50=0.13uM
BS02 ZN A 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:4zuq, PDBe:4zuq, PDBj:4zuq
PDBsum4zuq
PubMed26200446
UniProtQ48935|APAH_MYCRA Acetylpolyamine amidohydrolase (Gene Name=aphA)

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