Structure of PDB 4buz Chain A Binding Site BS01

Receptor Information
>4buz Chain A (length=237) Species: 2336 (Thermotoga maritima) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
MKMKEFLDLLNESRLTVTLTGAGISTPSGIPDFYSQNVFDIDFFYSHPEE
FYRFAKEGIFPMLQAKPNLAHVLLAKLEEKGLIEAVITQNIDRLHQRAGS
KKVIELHGNVEEYYCVRCEKKYTVEDVIKKLESSDVPLCDDCNSLIRPNI
VFFGENLPQDALREAIGLSSRASLMIVLGSSLVVYPAAELPLITVRSGGK
LVIVNLGETPFDDIATLKYNMDVVEFARRVMEEGGIS
Ligand information
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
PDB4buz Ex-527 Inhibits Sirtuins by Exploiting Their Unique Nad+-Dependent Deacetylation Mechanism
Resolution1.9 Å
Binding residue
(original residue number in PDB)
H116 V160 G163 E164 N165 L166 V192 V193 Y194 P195
Binding residue
(residue number reindexed from 1)
H107 V151 G154 E155 N156 L157 V183 V184 Y185 P186
Enzymatic activity
Catalytic site (original residue number in PDB) P31 D32 F33 N99 D101 H116
Catalytic site (residue number reindexed from 1) P31 D32 F33 N90 D92 H107
Enzyme Commision number 2.3.1.286: protein acetyllysine N-acetyltransferase.
Gene Ontology
Molecular Function
GO:0008270 zinc ion binding
GO:0016740 transferase activity
GO:0017136 NAD-dependent histone deacetylase activity
GO:0034979 NAD-dependent protein lysine deacetylase activity
GO:0046872 metal ion binding
GO:0051287 NAD binding
GO:0070403 NAD+ binding
Biological Process
GO:0006338 chromatin remodeling
GO:0006476 protein deacetylation
Cellular Component
GO:0005737 cytoplasm

View graph for
Molecular Function

View graph for
Biological Process

View graph for
Cellular Component
External links
PDB RCSB:4buz, PDBe:4buz, PDBj:4buz
PDBsum4buz
PubMed23840057
UniProtQ9WYW0|NPD_THEMA NAD-dependent protein deacetylase (Gene Name=cobB)

[Back to BioLiP]