Structure of PDB 1m2j Chain A

Receptor sequence
>1m2jA (length=249) Species: 2234 (Archaeoglobus fulgidus) [Search protein sequence]
MDEKLLKTIAESKYLVALTGAGVSAESGIPTFRGKDGLWNRYRPEELANP
QAFAKDPEKVWKWYAWRMEKVFNAQPNKANQAFAELERLGVLKCLITQNV
DDLHERAGSRNVIHLHGSLRVVRCTSCNNSFEVESAPKIPPLPKCDKCGS
LLRPGVVWFGEMLPPDVLDRAMREVERADVIIVAGTSAVVQPAASLPLIV
KQRGGAIIEINPDETPLTPIADYSLRGKAGEVMDELVRHVRKALSLKLN
3D structure
PDB1m2j Structural basis for the NAD-dependent deacetylase mechanism of Sir2
ChainA
Resolution1.7 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) P30 T31 F32 R33 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 C145 C124 C127 C145
BS02 APR A G20 A21 G22 E26 F32 R33 Q98 H116 G185 T186 S187 V190 N211 P212 D213 K228 A229 G20 A21 G22 E26 F32 R33 Q98 H116 G185 T186 S187 V190 N211 P212 D213 K228 A229
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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External links
PDB RCSB:1m2j, PDBe:1m2j, PDBj:1m2j
PDBsum1m2j
PubMed12091395
UniProtO28597|NPD1_ARCFU NAD-dependent protein deacylase 1 (Gene Name=cobB1)

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