Structure of PDB 2h59 Chain A

Receptor sequence

>2h59A (length=246) Species: 2336 (Thermotoga maritima)

MKMKEFLDLLNESRLTVTLTGAGISTPSGIPDFRGPNGIYKKYSQNVFDI
DFFYSHPEEFYRFAKEGIFPMLQAKPNLAHVLLAKLEEKGLIEAVITQNI
DRLHQRAGSKKVIELAGNVEEYYCVRCEKKYTVEDVIKKLESSDVPLCDD
CNSLIRPNIVFFGENLPQDALREAIGLSSRASLMIVLGSSLVVYPAAELP
LITVRSGGKLVIVNLGETPFDDIATLKYNMDVVEFARRVMEEGGIS

3D structure

• PDB: 2h59 Insights into the Sirtuin Mechanism from Ternary Complexes Containing NAD(+) and Acetylated Peptide.
• Chain: A
• Resolution: 1.9 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): P31 D32 F33 R34 N99 D101 A116
• Catalytic site (residue number reindexed from 1): P31 D32 F33 R34 N99 D101 A116
• 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	F162 G163 E164 N165 L166 V192 V193 Y194	F162 G163 E164 N165 L166 V192 V193 Y194
BS02	ZN	A	C124 C127 C148 C151	C124 C127 C148 C151
BS03	APR	A	G21 A22 G23 T26 P27 D32 F33 R34 Y40 Q98 F162 G188 S189 S190 V193 N214 L215 D231 V232	G21 A22 G23 T26 P27 D32 F33 R34 Y40 Q98 F162 G188 S189 S190 V193 N214 L215 D231 V232

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

External links

• PDB: RCSB:2h59, PDBe:2h59, PDBj:2h59
• PDBsum: 2h59
• PubMed: 16905097
• UniProt: Q9WYW0|NPD_THEMA NAD-dependent protein deacetylase (Gene Name=cobB)