Structure of PDB 4l3o Chain C

Receptor sequence
>4l3oC (length=294) Species: 9606 (Homo sapiens) [Search protein sequence]
RLLDELTLEGVARYMQSERCRRVICLVGAGISTSAGIPDFRSPNLEKYHL
PYPEAIFEISYFKKHPEPFFALAKELYPGQFKPTICHYFMRLLKDKGLLL
RCYTQNIDTLERIAGLEQEDLVEAHGTFYTSHCVSASCRHEYPLSWMKEK
IFSEVTPKCEDCQSLVKPDIVFFGESLPARFFSCMQSDFLKVDLLLVMGT
SLQVQPFASLISKAPLSTPRLLINKEKAGQSDPFLGMIMGLGGGMDFDSK
KAYRDVAWLGECDQGCLALAELLGWKKELEDLVRREHASIDAQS
3D structure
PDB4l3o Structural Basis for Potent Inhibition of SIRT2 Deacetylase by a Macrocyclic Peptide Inducing Dynamic Structural Change
ChainC
Resolution2.518 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) P94 D95 F96 R97 N168 D170 H187
Catalytic site (residue number reindexed from 1) P38 D39 F40 R41 N106 D108 H125
Enzyme Commision number 2.3.1.-
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 C E116 F119 H187 V233 F234 F235 G236 E237 L239 F244 Q265 V266 Q267 P268 S271 D294 F296 G298 M299 E54 F57 H125 V171 F172 F173 G174 E175 L177 F182 Q203 V204 Q205 P206 S209 D232 F234 G236 M237
BS02 ZN C C195 C200 C221 C133 C138 C159
Gene Ontology
Molecular Function
GO:0017136 NAD-dependent histone deacetylase activity
GO:0051287 NAD binding
GO:0070403 NAD+ binding

View graph for
Molecular Function
External links
PDB RCSB:4l3o, PDBe:4l3o, PDBj:4l3o
PDBsum4l3o
PubMed24389023
UniProtQ8IXJ6|SIR2_HUMAN NAD-dependent protein deacetylase sirtuin-2 (Gene Name=SIRT2)

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