Structure of PDB 2h2i Chain A

Receptor sequence
>2h2iA (length=244) Species: 2336 (Thermotoga maritima) [Search protein sequence]
MKMKEFLDLLNESRLTVTLTGAGISTPSGIPDFRGPNGIYKKYSQNVFDI
DFFYSHPEEFYRFAKEGIFPMLQAKPNLAHVLLAKLEEKGLIEAVITQNI
DRLHQRAGSKKVIELHGNVEEYYCVRCEKKYTVEDVIKKLESSDVPLCDD
CNSLIRPNIVFFGENLPQDALREAIGLSSRASLMIVLGSSLVVYPAAELP
LITVRSGGKLVIVNLGETPFDDIATLKYNMDVVEFARRVMEEGG
3D structure
PDB2h2i The structural basis of sirtuin substrate affinity
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 R34 N99 D101 H116
Catalytic site (residue number reindexed from 1) P31 D32 F33 R34 N99 D101 H116
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 ZN A C124 C127 C148 C151 C124 C127 C148 C151
BS02 ZPG A F48 I68 H116 V160 F162 L166 Y194 F48 I68 H116 V160 F162 L166 Y194
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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Biological Process

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Cellular Component
External links
PDB RCSB:2h2i, PDBe:2h2i, PDBj:2h2i
PDBsum2h2i
PubMed16768447
UniProtQ9WYW0|NPD_THEMA NAD-dependent protein deacetylase (Gene Name=cobB)

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