1Q14: HST2 protein

Structure and autoregulation of the yeast Hst2 homolog of Sir2. Determined by X-ray diffraction at 2.5 Å resolution. Released 30 Sept 2003.

Method: X-ray diffraction
Resolution: 2.5 Å
Organism: Saccharomyces cerevisiae
Chains: 1
Atoms: 2,411
Mol. weight: 40.48 kDa
Ligands: ZN
Released: 30 Sept 2003

Explore 1Q14 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1Q14 contains 19 α-helices and 13 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: 19 helices, 13 β-strands

Element	Residues	Length	Sheet
α-helix	8-20	13
β-strand	27-31	5	1
α-helix	33-35	3
α-helix	37-39	3
α-helix	63-67	5
β-strand	68	1	2
α-helix	69-74	6
α-helix	77-83	7
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	153-158	6
β-strand	169	1	4
β-strand	176	1	4
β-strand	177-181	5	3
α-helix	182-183	2
β-strand	184	1	2
α-helix	187-189	3
α-helix	190-205	16
β-strand	218-222	5	1
α-helix	231-233	3
α-helix	234-237	4
β-strand	243-247	5	1
α-helix	253-257	5
β-strand	264-266	3	1
α-helix	270-281	12
α-helix	284-293	10
α-helix	304-313	10

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
HST2 protein	A	protein	361	Saccharomyces cerevisiae	P53686 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>1Q14_1 HST2 protein (chains A)
GMASMSVSTASTEMSVRKIAAHMKSNPNAKVIFMVGAGISTSCGIPDFRSPGTGLYHNLA
RLKLPYPEAVFDVDFFQSDPLPFYTLAKELYPGNFRPSKFHYLLKLFQDKDVLKRVYTQN
IDTLERQAGVKDDLIIEAHGSFAHCHCIGCGKVYPPQVFKSKLAEHPIKDFVKCDVCGEL
VKPAIVFFGEDLPDSFSETWLNDSEWLREKITTSGKHPQQPLVIVVGTSLAVYPFASLPE
EIPRKVKRVLCNLETVGDFKANKRPTDLIVHQYSDEFAEQLVEELGWQEDFEKILTAQGG
MGDNSKEQLLEIVHDLENLSLDQSEHESADKKDKKLQRLNGHDSDEDGASNSSSSQKAAK
E

Ligands and cofactors

ID	Name	Formula	Copies
ZN	Zinc ion	Zn	1

Water and common crystallization additives (CL) are not listed.

Primary citation

Structure and autoregulation of the Yeast Hst2 homolog of Sir2. Zhao, K., Chai, X., Clements, A. et al. Nat Struct Biol (2003) 10:864-871. DOI 10.1038/nsb978 · 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
7F51 1.98 Å, Crystal structure of Hst2 in complex with 2'-O-Benzoyl ADP Ribose
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
1Q17 2.7 Å, Structure of the yeast Hst2 protein deacetylase in ternary complex with 2'-O-acetyl ADP…

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