7LO0: Human ASF1a

Structure of human ASF1a in complex with a TLK2 peptide. Determined by X-ray diffraction at 2.71 Å resolution. Released 16 Feb 2022.

Method: X-ray diffraction
Resolution: 2.71 Å
Organism: Homo sapiens
Chains: 24
Atoms: 11,548
Mol. weight: 182.64 kDa
Released: 16 Feb 2022

Explore 7LO0 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

7LO0 contains 65 α-helices and 93 β-strands across 24 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	4-11	8	1
β-strand	16-17	2	2
α-helix	21	1
β-strand	22-30	9	1
β-strand	38-45	8	2
α-helix	51-53	3
β-strand	54-61	8	2
β-strand	69-76	8	1
α-helix	77-79	3
α-helix	81-83	3
α-helix	86-89	4
β-strand	91-101	11	2
β-strand	104-117	14	2
α-helix	120-124	5
α-helix	132-134	3
β-strand	135-139	5	2
β-strand	145-148	4	2

Chain B: 7 helices, 9 β-strands

Element	Residues	Length	Sheet
β-strand	4-11	8	3
β-strand	15-17	3	4
α-helix	21	1
β-strand	22-30	9	3
β-strand	38-45	8	4
α-helix	51-53	3
β-strand	54-62	9	4
β-strand	68-76	9	3
α-helix	77-79	3
α-helix	81-83	3
α-helix	86-89	4
β-strand	91-101	11	4
β-strand	104-117	14	4
α-helix	120-124	5
α-helix	132-134	3
β-strand	135-148	14	4

Chain C: 6 helices, 12 β-strands

Element	Residues	Length	Sheet
β-strand	4-11	8	5
β-strand	16-17	2	6
α-helix	21	1
β-strand	22-30	9	5
β-strand	34	1	7
β-strand	38-45	8	6
α-helix	51-53	3
β-strand	54-62	9	6
β-strand	65	1	7
β-strand	68-76	9	5
α-helix	77-79	3
α-helix	81-83	3
α-helix	86-89	4
β-strand	91-101	11	6
β-strand	104-117	14	6
α-helix	120-124	5
β-strand	135-139	5	6
β-strand	145-148	4	6

Chain D: 7 helices, 12 β-strands

Element	Residues	Length	Sheet
β-strand	4-11	8	8
β-strand	16-17	2	9
α-helix	21	1
β-strand	22-30	9	8
β-strand	34	1	10
α-helix	37	1
β-strand	38-45	8	9
α-helix	51-53	3
β-strand	54-62	9	9
β-strand	65	1	10
β-strand	68-76	9	8
α-helix	77-79	3
α-helix	81-83	3
α-helix	86-89	4
β-strand	91-101	11	9
β-strand	104-117	14	9
α-helix	120-124	5
β-strand	135-139	5	9
β-strand	145-148	4	9

Chains E and H: 7 helices, 10 β-strands

Element	Residues	Length	Sheet
β-strand	4-11	8	11
β-strand	16-17	2	12
α-helix	21	1
β-strand	22-30	9	11
β-strand	38-45	8	12
α-helix	51-53	3
β-strand	54-62	9	12
β-strand	68-76	9	11
α-helix	77-79	3
α-helix	81-83	3
α-helix	86-89	4
β-strand	91-101	11	12
β-strand	104-117	14	12
α-helix	120-124	5
α-helix	132-134	3
β-strand	135-139	5	12
β-strand	145-148	4	12

Chain F: 8 helices, 12 β-strands

Element	Residues	Length	Sheet
β-strand	4-12	9	13
β-strand	15-17	3	14
α-helix	21	1
β-strand	22-30	9	13
β-strand	34	1	15
β-strand	38-45	8	14
α-helix	51-53	3
β-strand	54-62	9	14
β-strand	65	1	15
α-helix	66	1
β-strand	68-76	9	13
α-helix	77-79	3
α-helix	81-83	3
α-helix	86-89	4
β-strand	91-101	11	14
β-strand	104-117	14	14
α-helix	120-124	5
α-helix	132-134	3
β-strand	135-139	5	14
β-strand	145-148	4	14

Chain G: 8 helices, 10 β-strands

Element	Residues	Length	Sheet
β-strand	4-12	9	16
β-strand	16-17	2	17
α-helix	21	1
β-strand	22-30	9	16
β-strand	38-45	8	17
α-helix	51-53	3
β-strand	54-62	9	17
α-helix	64-66	3
β-strand	68-76	9	16
α-helix	77-79	3
α-helix	81-83	3
α-helix	86-89	4
β-strand	91-101	11	17
β-strand	104-117	14	17
α-helix	120-124	5
α-helix	132-134	3
β-strand	135-139	5	17
β-strand	145-148	4	17

Chains I, J, K, N, O and P: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	10-21	12

4 more chain groups are not listed. Open the entry in the viewer and use the sequence panel to see them.

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Histone chaperone ASF1A	A, B, C, D, E, F, G, H	protein	157	Homo sapiens	Q9Y294 (AlphaFold model)
Serine/threonine-protein kinase tousled-like 2	I, J, K, L, M, N, O, P, Q, R, T, U, V, W, X, Y	protein	21	Homo sapiens	Q86UE8 (AlphaFold model)

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

>7LO0_1 Histone chaperone ASF1A (chains A, B, C, D, E, F, G, H)
GSMAKVQVNNVVVLDNPSPFYNPFQFEITFECIEDLSEDLEWKIIYVGSAESEEYDQVLD
SVLVGPVPAGRHMFVFQADAPNPGLIPDADAVGVTVVLITCTYRGQEFIRVGYYVNNEYT
ETELRENPPVKPDFSKLQRNILASNPRVTRFHINWED

Sequence of entity 2 (I, J, K, L, M, N, O, P, Q, R, T, U, V, W, X, Y), FASTA

>7LO0_2 Serine/threonine-protein kinase tousled-like 2 (chains I, J, K, L, M, N, O, P, Q, R, T, U, V, W, X, Y)
EELHSLDPRRQELLEARFTGV

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
7LNY 2.1 Å, Apo structure of the Histone chaperone ASF1A residues 1-155
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…

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