Structure of PDB 3pdh Chain A

Receptor sequence
>3pdhA (length=237) Species: 2336 (Thermotoga maritima) [Search protein sequence]
MKMKEFLDLLNESRLTVTLTGAGISTPSGIPDFYSQNVFDIDFFYSHPEE
FYRFAKEGIFPMLQAKPNLAHVLLAKLEEKGLIEAVITQNIDRLHQRAGS
KKVIELHGNVEEYYCVRCEKKYTVEDVIKKLESSDVPLCDDCNSLIRPNI
VFFGENLPQDALREAIGLSSRASLMIVLGSSLVVYPAAELPLITVRSGGK
LVIVNLGETPFDDIATLKYNMDVVEFARRVMEEGGIS
3D structure
PDB3pdh Structure of Sir2Tm bound to a propionylated peptide.
ChainA
Resolution1.8 Å
3D
structure
Catalytic site residues are labeled in the structure
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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.
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 peptide A F48 H116 V160 F162 G163 E164 N165 L166 V192 V193 Y194 P195 F39 H107 V151 F153 G154 E155 N156 L157 V183 V184 Y185 P186
BS02 ZN A C124 C127 C148 C151 C115 C118 C139 C142
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

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Molecular Function
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Cellular Component
External links
PDB RCSB:3pdh, PDBe:3pdh, PDBj:3pdh
PDBsum3pdh
PubMed21080423
UniProtQ9WYW0|NPD_THEMA NAD-dependent protein deacetylase (Gene Name=cobB)

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