5BT1: HAT1-interacting factor 1

Name: PDB 5BT1: histone chaperone Hif1 playing with histone H2A-H2B dimer
Published: 2016-10-26
License: https://creativecommons.org/publicdomain/zero/1.0/
Keywords: chaperone

histone chaperone Hif1 playing with histone H2A-H2B dimer. Determined by X-ray diffraction at 2.62 Å resolution. Released 26 Oct 2016.

Method: X-ray diffraction
Resolution: 2.62 Å
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Chains: 4
Atoms: 5,317
Mol. weight: 120 kDa
Released: 26 Oct 2016

Explore 5BT1 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

5BT1 contains 40 α-helices and 4 β-strands across 4 chains. 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: 14 helices, 0 β-strands

Element	Residues	Length
α-helix	18-20	3
α-helix	22-34	13
α-helix	38-51	14
α-helix	58-60	3
α-helix	62-77	16
α-helix	186-188	3
α-helix	194-198	5
α-helix	202-217	16
α-helix	225-228	4
α-helix	229-249	21
α-helix	252-266	15
α-helix	273-290	18
α-helix	298-316	19
α-helix	323-342	20

Chain B: 17 helices, 0 β-strands

Element	Residues	Length
α-helix	22-34	13
α-helix	38-51	14
α-helix	58-60	3
α-helix	62-79	18
α-helix	167-171	5
α-helix	186-188	3
α-helix	194-198	5
α-helix	202-217	16
α-helix	219-221	3
α-helix	225-228	4
α-helix	229-248	20
α-helix	252-266	15
α-helix	270-271	2
α-helix	273-289	17
α-helix	290-292	3
α-helix	298-316	19
α-helix	323-342	20

Chain C: 5 helices, 2 β-strands

Element	Residues	Length	Sheet
α-helix	18-22	5
α-helix	28-36	9
β-strand	43-44	2	1
α-helix	47-73	27
β-strand	78-79	2	2
α-helix	81-89	9
α-helix	92-98	7

Chain D: 4 helices, 2 β-strands

Element	Residues	Length	Sheet
α-helix	41-51	11
β-strand	56-57	2	2
α-helix	59-86	28
β-strand	91-92	2	1
α-helix	94-104	11
α-helix	107-125	19

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
HAT1-interacting factor 1	A, B	protein	393	Saccharomyces cerevisiae (strain ATCC 204508 / S288c)	Q12373 (AlphaFold model)
Histone H2A.1	C	protein	143	Saccharomyces cerevisiae (strain ATCC 204508 / S288c)	P04911 (AlphaFold model)
Histone H2B.1	D	protein	142	Saccharomyces cerevisiae (strain ATCC 204508 / S288c)	P02293 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>5BT1_1 HAT1-interacting factor 1 (chains A, B)
MKLRAEDVLANGTSRHKVQIDMERQVQIAKDLLAQKKFLEAAKRCQQTLDSLPKDGLLPD
PELFTIFAQAVYNMEVQNSGNLFGDALLAGDDGSGSESESEPESDVSNGEEGNENGQTEI
PNSRMFQFDQEEEDLTGDVDSGDSEDSGEGSEEEEENVEKEEERLALHELANFSPANEHD
DEIEDVSQLRKSGFHIYFENDLYENALDLLAQALMLLGRPTADGQSLTENSRLRIGDVYI
LMGDIEREAEMFSRAIHHYLKALGYYKTLKPAEQVTEKVIQAEFLVCDALRWVDQVPAKD
KLKRFKHAKALLEKHMTTRPKDSELQQARLAQIQDDIDEVQENQQHGSKRPLSQPTTSIG
FPALEKPLGDFNDLSQLVKKKPRRHLEHHHHHH

Sequence of entity 2 (C), FASTA

>5BT1_2 Histone H2A.1 (chains C)
MGHHHHHHGSHMSGGKGGKAGSAAKASQSRSAKAGLTFPVGRVHRLLRRGNYAQRIGSGA
PVYLTAVLEYLAAEILELAGNAARDNKKTRIIPRHLQLAIRNDDELNKLLGNVTIAQGGV
LPNIHQNLLPKKSAKATKASQEL

Sequence of entity 3 (D), FASTA

>5BT1_3 Histone H2B.1 (chains D)
MGHHHHHHGSHMSAKAEKKPASKAPAEKKPAAKKTSTSTDGKKRSKARKETYSSYIYKVL
KQTHPDTGISQKSMSILNSFVNDIFERIATEASKLAAYNKKSTISAREIQTAVRLILPGE
LAKHAVSEGTRAVTKYSSSTQA

Primary citation

Structural Insights into the Association of Hif1 with Histones H2A-H2B Dimer and H3-H4 Tetramer. Zhang, M., Liu, H., Gao, Y. et al. Structure (2016) 24:1810-1820. DOI 10.1016/j.str.2016.08.001 · PubMed

Other PDB entries of the same protein (UniProt Q12373 (AlphaFold model), which also has an AlphaFold model), best resolution first:

4NQ0 2.1 Å, Structural insights into yeast histone chaperone Hif1: a scaffold protein recruiting…

Browse structure collections

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