Structure of PDB 1s7g Chain A

Receptor sequence
>1s7gA (length=252) Species: 2234 (Archaeoglobus fulgidus) [Search protein sequence]
MEDEIRKAAEILAKSKHAVVFTGAGISAESGIPTFRGEDGLWRKYDPEEV
ASISGFKRNPRAFWEFSMEMKDKLFAEPNPAHYAIAELERMGIVKAVITQ
NIDMLHQRAGSRRVLELHGSMDKLDCLDCHETYDWSEFVEDFNKGEIPRC
RKCGSYYVKPRVVLFGEPLPQRTLFEAIEEAKHCDAFMVVGSSLVVYPAA
ELPYIAKKAGAKMIIVNAEPTMADPIFDVKIIGKAGEVLPKIVEEVKRLR
SE
3D structure
PDB1s7g Structural basis for the mechanism and regulation of sir2 enzymes
ChainA
Resolution2.3 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) P33 T34 F35 R36 N101 D103 H118
Catalytic site (residue number reindexed from 1) P33 T34 F35 R36 N101 D103 H118
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 C126 C129 C150 C153 C126 C129 C150 C153
BS02 ZN A H17 E180 H183 H17 E180 H183
BS03 NAD A G23 G25 T34 Q100 G191 S192 S193 N217 A218 E219 K234 A235 G23 G25 T34 Q100 G191 S192 S193 N217 A218 E219 K234 A235
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:0036054 protein-malonyllysine demalonylase activity
GO:0036055 protein-succinyllysine desuccinylase activity
GO:0046872 metal ion binding
GO:0051287 NAD binding
GO:0070403 NAD+ binding
Biological Process
GO:0006338 chromatin remodeling
GO:0006476 protein deacetylation
GO:0036049 peptidyl-lysine desuccinylation
Cellular Component
GO:0005737 cytoplasm

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Cellular Component
External links
PDB RCSB:1s7g, PDBe:1s7g, PDBj:1s7g
PDBsum1s7g
PubMed15023335
UniProtO30124|NPD2_ARCFU NAD-dependent protein deacylase 2 (Gene Name=cobB2)

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