7LNY: Histone chaperone ASF1A

Apo structure of the Histone chaperone ASF1A residues 1-155. Determined by X-ray diffraction at 2.1 Å resolution. Released 16 Feb 2022.

Method: X-ray diffraction
Resolution: 2.1 Å
Organism: Homo sapiens
Chains: 7
Atoms: 9,138
Mol. weight: 124.81 kDa
Released: 16 Feb 2022

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

Secondary structure: helices and β-sheets

7LNY contains 50 α-helices and 75 β-strands across 7 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: 7 helices, 10 β-strands

Element	Residues	Length	Sheet
β-strand	6-13	8	1
β-strand	17-19	3	2
α-helix	23	1
β-strand	24-32	9	1
β-strand	40-47	8	2
α-helix	53-55	3
β-strand	56-64	9	2
β-strand	70-78	9	1
α-helix	79-81	3
α-helix	83-85	3
α-helix	88-91	4
β-strand	93-103	11	2
β-strand	106-119	14	2
α-helix	122-126	5
α-helix	134-136	3
β-strand	137-141	5	2
β-strand	147-150	4	2

Chain B: 7 helices, 10 β-strands

Element	Residues	Length	Sheet
β-strand	6-13	8	3
β-strand	18-19	2	4
α-helix	23	1
β-strand	24-32	9	3
β-strand	36-47	12	4
α-helix	53-55	3
β-strand	56-67	12	4
β-strand	70-78	9	3
α-helix	79-81	3
α-helix	83-85	3
α-helix	88-91	4
β-strand	93-103	11	4
β-strand	106-119	14	4
α-helix	122-126	5
α-helix	134-136	3
β-strand	137-141	5	4
β-strand	147-150	4	4

Chain C: 7 helices, 12 β-strands

Element	Residues	Length	Sheet
β-strand	6-13	8	5
β-strand	18-19	2	1
α-helix	23	1
β-strand	24-32	9	5
β-strand	36	1	6
β-strand	40-47	8	1
α-helix	53-55	3
β-strand	56-64	9	1
β-strand	67	1	6
β-strand	70-78	9	5
α-helix	79-81	3
α-helix	83-85	3
α-helix	88-91	4
β-strand	93-103	11	1
β-strand	106-119	14	1
α-helix	122-126	5
α-helix	134-136	3
β-strand	137-141	5	1
β-strand	147-150	4	1

Chain D: 7 helices, 12 β-strands

Element	Residues	Length	Sheet
β-strand	6-13	8	7
β-strand	17-19	3	8
α-helix	23	1
β-strand	24-32	9	7
β-strand	36	1	9
α-helix	39	1
β-strand	40-47	8	8
α-helix	53-55	3
β-strand	56-64	9	8
β-strand	67	1	9
β-strand	70-78	9	7
α-helix	79-81	3
α-helix	83-85	3
α-helix	88-91	4
β-strand	93-103	11	8
β-strand	106-119	14	8
α-helix	122-126	5
β-strand	137-141	5	8
β-strand	147-150	4	8

Chain E: 7 helices, 12 β-strands

Element	Residues	Length	Sheet
β-strand	6-12	7	10
β-strand	17-19	3	3
α-helix	23	1
β-strand	24-32	9	10
β-strand	36	1	11
β-strand	40-47	8	3
α-helix	53-55	3
β-strand	56-64	9	3
β-strand	67	1	11
β-strand	70-78	9	10
α-helix	79-82	4
α-helix	83-85	3
α-helix	88-91	4
β-strand	93-103	11	3
β-strand	106-119	14	3
α-helix	122-126	5
α-helix	134-136	3
β-strand	137-141	5	3
β-strand	147-150	4	3

Chain F: 7 helices, 10 β-strands

Element	Residues	Length	Sheet
β-strand	6-13	8	12
β-strand	18-19	2	13
α-helix	23	1
β-strand	24-32	9	12
β-strand	40-47	8	13
α-helix	53-55	3
β-strand	56-63	8	13
β-strand	70-78	9	12
α-helix	79-82	4
α-helix	83-85	3
α-helix	88-90	3
β-strand	93-103	11	13
β-strand	106-119	14	13
α-helix	122-126	5
α-helix	134-136	3
β-strand	137-141	5	13
β-strand	147-150	4	13

Chain G: 8 helices, 9 β-strands

Element	Residues	Length	Sheet
β-strand	6-13	8	14
β-strand	17-19	3	15
α-helix	23	1
β-strand	24-32	9	14
α-helix	39	1
β-strand	40-47	8	15
α-helix	53-55	3
β-strand	56-64	9	15
β-strand	70-78	9	14
α-helix	79-81	3
α-helix	83-85	3
α-helix	88-91	4
β-strand	93-103	11	15
β-strand	106-119	14	15
α-helix	122-126	5
α-helix	134-136	3
β-strand	137-150	14	15

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Histone chaperone ASF1A	A, B, C, D, E, F, G	protein	157	Homo sapiens	Q9Y294 (AlphaFold model)

Sequence of entity 1 (A, B, C, D, E, F, G), FASTA

>7LNY_1 Histone chaperone ASF1A (chains A, B, C, D, E, F, G)
GSMAKVQVNNVVVLDNPSPFYNPFQFEITFECIEDLSEDLEWKIIYVGSAESEEYDQVLD
SVLVGPVPAGRHMFVFQADAPNPGLIPDADAVGVTVVLITCTYRGQEFIRVGYYVNNEYT
ETELRENPPVKPDFSKLQRNILASNPRVTRFHINWED

Primary citation

Tousled-like kinase 2 targets ASF1 histone chaperones through client mimicry. Simon, B., Lou, H.J., Huet-Calderwood, C. et al. Nat Commun (2022) 13:749-749. DOI 10.1038/s41467-022-28427-0 · PubMed

Other PDB entries of the same protein (UniProt Q9Y294 (AlphaFold model), which also has an AlphaFold model), best resolution first:

9SVO 1.6 Å, Crystal structure hASF1A 156-cr5
9TRB 1.65 Å, Crystal structure hASF1A 156-cr13
9SQK 1.7 Å, Crystal structure hASF1A 156-cr17
6ZUF 1.8 Å, Urea-based Foldamer Inhibitor chimera C2 in complex with ASF1 Histone chaperone
6F0H 1.98 Å, Crystal structure ASF1-ip4
9SS3 2.0 Å, Crystal structure hASF1A 156-cr7
6F0F 2.0 Å, Crystal structure ASF1-ip2_s
8CJ2 2.13 Å, Urea-based foldamer inhibitor c3u_5 chimera in complex with ASF1 histone chaperone
6F0G 2.3 Å, Crystal structure ASF1-ip3
8CJ1 2.56 Å, Urea-based foldamer inhibitor c3u_3 chimera in complex with ASF1 histone chaperone
2I32 2.7 Å, Structure of a human ASF1a-HIRA complex and insights into specificity of histone…
2IO5 2.7 Å, Crystal structure of the CIA- histone H3-H4 complex

Browse structure collections

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