Structure of PDB 1ici Chain B

Receptor sequence
>1iciB (length=244) Species: 2234 (Archaeoglobus fulgidus) [Search protein sequence]
DEKLLKTIAESKYLVALTGAGVSAESGIPTFRGKDGLWNRYRPEELANPQ
AFAKDPEKVWKWYAWRMEKVFNAQPNKAHQAFAELERLGVLKCLITQNVD
DLHERAGSRNVIHLHGSLRVVRCTSCNNSFEVESAPKIPPLPKCDKCGSL
LRPGVVWFGEMLPPDVLDRAMREVERADVIIVAGTSAVVQPAASLPLIVK
QRGGAIIEINPDETPLTPIADYSLRGKAGEVMDELVRHVRKALS
3D structure
PDB1ici Crystal structure of a SIR2 homolog-NAD complex.
ChainB
Resolution2.1 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) P30 T31 F32 R33 N99 D101 H116
Catalytic site (residue number reindexed from 1) P29 T30 F31 R32 N98 D100 H115
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 B C124 C127 C145 C148 C123 C126 C144 C147
BS02 NAD B G20 A21 G22 E26 F32 P44 Q98 H116 G185 T186 S187 V190 N211 P212 D213 K228 A229 G19 A20 G21 E25 F31 P43 Q97 H115 G184 T185 S186 V189 N210 P211 D212 K227 A228
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:0070403 NAD+ binding
Biological Process
GO:0006338 chromatin remodeling
GO:0006476 protein deacetylation
GO:0036048 protein desuccinylation
GO:0036049 peptidyl-lysine desuccinylation
Cellular Component
GO:0005737 cytoplasm

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Cellular Component
External links
PDB RCSB:1ici, PDBe:1ici, PDBj:1ici
PDBsum1ici
PubMed11336676
UniProtO28597|NPD1_ARCFU NAD-dependent protein deacylase 1 (Gene Name=cobB1)

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