7F51: Hst2

Crystal structure of Hst2 in complex with 2'-O-Benzoyl ADP Ribose. Determined by X-ray diffraction at 1.98 Å resolution. Released 16 Mar 2022.

Method: X-ray diffraction
Resolution: 1.98 Å
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Chains: 1
Atoms: 2,495
Mol. weight: 33.25 kDa
Ligands: ZN, BA7
Released: 16 Mar 2022

Explore 7F51 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

7F51 contains 20 α-helices and 15 β-strands across 1 chain. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 20 helices, 15 β-strands

Element	Residues	Length	Sheet
α-helix	9-21	13
β-strand	27-31	5	1
α-helix	33-35	3
α-helix	37-39	3
α-helix	41-43	3
α-helix	51-59	9
α-helix	63-67	5
β-strand	68	1	2
α-helix	69-74	6
α-helix	77-86	10
α-helix	92-94	3
α-helix	95-105	11
β-strand	109-114	6	1
α-helix	120-123	4
α-helix	128-130	3
β-strand	131-133	3	1
β-strand	136-143	8	3
β-strand	149-150	2	3
α-helix	152-158	7
β-strand	169	1	4
β-strand	176	1	4
β-strand	177-181	5	3
β-strand	184	1	2
α-helix	187-189	3
α-helix	190-203	14
β-strand	208	1	5
β-strand	214	1	5
β-strand	218-222	5	1
α-helix	231-233	3
α-helix	234-237	4
β-strand	243-247	5	1
α-helix	254-257	4
β-strand	264-266	3	1
α-helix	270-281	12
α-helix	284-293	10

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
NAD-dependent protein deacetylase HST2	A	protein	287	Saccharomyces cerevisiae (strain ATCC 204508 / S288c)	P53686 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>7F51_1 NAD-dependent protein deacetylase HST2 (chains A)
TEMSVRKIAAHMKSNPNAKVIFMVGAGISTSCGIPDFRSPGTGLYHNLARLKLPYPEAVF
DVDFFQSDPLPFYTLAKELYPGNFRPSKFHYLLKLFQDKDVLKRVYTQNIDTLERQAGVK
DDLIIEAHGSFAHCHCIGCGKVYPPQVFKSKLAEHPIKDFVKCDVCGELVKPAIVFFGED
LPDSFSETWLNDSEWLREKITTSGKHPQQPLVIVVGTSLAVYPFASLPEEIPRKVKRVLC
NLETVGDFKANKRPTDLIVHQYSDEFAEQLVEELGWQEDFEKILTAQ

Ligands and cofactors

ID	Name	Formula	Copies
ZN	Zinc ion	Zn	1
BA7	[(2R,3R,4R,5R)-5-[[[[(2R,3S,4R,5R)-5-(6-aminopurin-9-yl)-3,4-bis(oxidanyl)oxola…	C22 H27 N5 O15 P2	1

Primary citation

Global profiling of regulatory elements in the histone benzoylation pathway. Wang, D., Yan, F., Wu, P. et al. Nat Commun (2022) 13:1369-1369. DOI 10.1038/s41467-022-29057-2 · PubMed

Other PDB entries of the same protein (UniProt P53686 (AlphaFold model), which also has an AlphaFold model), best resolution first:

1Q1A 1.5 Å, Structure of the yeast Hst2 protein deacetylase in ternary complex with 2'-O-acetyl ADP…
1SZD 1.5 Å, Structural basis for nicotinamide cleavage and ADP-ribose transfer by NAD+-dependent…
1SZC 1.75 Å, Structural basis for nicotinamide cleavage and ADP-ribose transfer by NAD+-dependent…
7F4E 1.78 Å, Crystal structure of Hst2 in complex with H3K9bz peptide
2OD2 2.0 Å, Crystal Structure of yHst2 I117F mutant bound to carba-NAD+ and an acetylated H4 peptide
2OD7 2.0 Å, Crystal Structure of yHst2 bound to the intermediate analogue ADP-HPD, and and aceylated…
2QQF 2.0 Å, Hst2 bound to ADP-HPD and Acetylated histone H4
2OD9 2.05 Å, Structural Basis for Nicotinamide Inhibition and Base Exchange in Sir2 Enzymes
2QQG 2.05 Å, Hst2 bound to ADP-HPD, acetyllated histone H4 and nicotinamide
1Q14 2.5 Å, Structure and autoregulation of the yeast Hst2 homolog of Sir2
1Q17 2.7 Å, Structure of the yeast Hst2 protein deacetylase in ternary complex with 2'-O-acetyl ADP…

Browse structure collections

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