Structure of PDB 1q17 Chain A

Receptor sequence
>1q17A (length=290) Species: 4932 (Saccharomyces cerevisiae) [Search protein sequence]
GMASMSVSTASTEMSVRKIAAHMKSNPNAKVIFMVGAGISTSCGIPDFRS
PGTGLYHNLARLKLPYPEAVFDVDFFQSDPLPFYTLAKELYPGNFRPSKF
HYLLKLFQDKDVLKRVYTQNIDTLERQAGVKDDLIIEAHGSFAHCHCIGC
GKVYPPQVFKSKLAEHPIKDFVKCDVCGELVKPAIVFFGEDLPDSFSETW
LNDSEWLREKIQPLVIVVGTSLAVYPFASLPEEIPRKVKRVLCNLETVGD
FKANKRPTDLIVHQYSDEFAEQLVEELGWQEDFEKILTAQ
3D structure
PDB1q17 Structure of the Yeast Hst2 Protein Deacetylase in Ternary Complex with 2'-O-Acetyl ADP Ribose and Histone Peptide.
ChainA
Resolution2.7 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) P42 D43 F44 R45 N116 D118 H135
Catalytic site (residue number reindexed from 1) P46 D47 F48 R49 N120 D122 H139
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 C143 C146 C170 C173 C147 C150 C174 C177
BS02 APR A G32 A33 G34 F44 R45 Y52 Q115 H135 G223 T224 S225 V228 N248 L249 E250 Y269 S270 G36 A37 G38 F48 R49 Y56 Q119 H139 G219 T220 S221 V224 N244 L245 E246 Y265 S266
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:1q17, PDBe:1q17, PDBj:1q17
PDBsum1q17
PubMed14604530
UniProtP53686|HST2_YEAST NAD-dependent protein deacetylase HST2 (Gene Name=HST2)

[Back to BioLiP]