Structure of PDB 1yc5 Chain A

Receptor sequence
>1yc5A (length=234) Species: 2336 (Thermotoga maritima) [Search protein sequence]
MKMKEFLDLLNESRLTVTLTGAGISTPSGIPDFQNVFDIDFFYSHPEEFY
RFAKEGIFPMLQAKPNLAHVLLAKLEEKGLIEAVITQNIDRLHQRAGSKK
VIELHGNVEEYYCVRCEKKYTVEDVIKKLESSDVPLCDDCNSLIRPNIVF
FGENLPQDALREAIGLSSRASLMIVLGSSLVVYPAAELPLITVRSGGKLV
IVNLGETPFDDIATLKYNMDVVEFARRVMEEGGI
3D structure
PDB1yc5 Mechanism of sirtuin inhibition by nicotinamide: altering the NAD(+) cosubstrate specificity of a Sir2 enzyme.
ChainA
Resolution1.4 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 N88 D90 H105
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 H116 V160 F162 G163 E164 N165 L166 V192 V193 Y194 P195 H105 V149 F151 G152 E153 N154 L155 V181 V182 Y183 P184
BS02 ZN A C124 C127 C148 C151 C113 C116 C137 C140
BS03 NCA A P31 F33 N99 I100 D101 P31 F33 N88 I89 D90 MOAD: ic50=1mM
PDBbind-CN: -logKd/Ki=3.00,IC50=1.0mM
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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Cellular Component
External links
PDB RCSB:1yc5, PDBe:1yc5, PDBj:1yc5
PDBsum1yc5
PubMed15780941
UniProtQ9WYW0|NPD_THEMA NAD-dependent protein deacetylase (Gene Name=cobB)

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