5C3I: Histone chaperone ASF1A

Crystal structure of the quaternary complex of histone H3-H4 heterodimer with chaperone ASF1 and the replicative helicase subunit MCM2. Determined by X-ray diffraction at 3.5 Å resolution. Released 29 Jul 2015.

Method: X-ray diffraction
Resolution: 3.5 Å
Organism: Homo sapiens
Chains: 24
Atoms: 17,655
Mol. weight: 347.73 kDa
Released: 29 Jul 2015

Explore 5C3I in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

5C3I contains 101 α-helices and 113 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: 8 helices, 12 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	34	1	3
α-helix	37	1
β-strand	38-45	8	2
α-helix	51-53	3
β-strand	54-62	9	2
β-strand	65	1	3
β-strand	68-76	9	1
α-helix	77-79	3
α-helix	81-83	3
α-helix	86-89	4
β-strand	92-101	10	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: 4 helices, 2 β-strands

Element	Residues	Length	Sheet
α-helix	49-57	9
α-helix	64-78	15
β-strand	83-84	2	4
α-helix	86-113	28
β-strand	118-119	2	5
α-helix	121-130	10

Chain C: 4 helices, 3 β-strands

Element	Residues	Length	Sheet
α-helix	25-28	4
α-helix	31-41	11
β-strand	45-46	2	5
α-helix	50-75	26
β-strand	80-81	2	4
α-helix	83-91	9
β-strand	95-98	4	2

Chain D: 2 helices, 3 β-strands

Element	Residues	Length	Sheet
β-strand	70-71	2	5
β-strand	95	1	4
α-helix	102-106	5
α-helix	107-120	14
β-strand	138-139	2	2

Chain E: 6 helices, 11 β-strands

Element	Residues	Length	Sheet
β-strand	4-11	8	6
β-strand	16-17	2	7
α-helix	21	1
β-strand	22-30	9	6
β-strand	34	1	8
β-strand	38-45	8	7
α-helix	51-53	3
β-strand	54-62	9	7
β-strand	65	1	8
β-strand	68-76	9	6
α-helix	77-79	3
α-helix	86-89	4
β-strand	92-101	10	7
β-strand	105-117	13	7
α-helix	120-124	5
α-helix	132-134	3
β-strand	135-148	14	7

Chain F: 3 helices, 4 β-strands

Element	Residues	Length	Sheet
β-strand	48-53	6	9
β-strand	56	1	10
α-helix	64-76	13
β-strand	83-84	2	11
α-helix	86-113	28
β-strand	119	1	12
α-helix	121-130	10

Chain G: 4 helices, 3 β-strands

Element	Residues	Length	Sheet
α-helix	26-28	3
α-helix	31-41	11
β-strand	45-47	3	12
α-helix	50-75	26
β-strand	80-81	2	11
α-helix	83-91	9
β-strand	95-98	4	7

Chain H: 2 helices, 3 β-strands

Element	Residues	Length	Sheet
β-strand	69-71	3	12
α-helix	77-80	4
β-strand	82	1	10
β-strand	95	1	11
α-helix	107-121	15

16 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, E, I, M, Q, U	protein	188	Homo sapiens	Q9Y294 (AlphaFold model)
Histone H3.1	B, F, J, N, R, V	protein	136	Homo sapiens	P68431 (AlphaFold model)
Histone H4	C, G, K, O, S, W	protein	103	Homo sapiens	P62805 (AlphaFold model)
DNA replication licensing factor MCM2,MCM2	D, H, L, P, T, X	protein	93	Homo sapiens	P49736 (AlphaFold model)

Sequence of entity 1 (A, E, I, M, Q, U), FASTA

>5C3I_1 Histone chaperone ASF1A (chains A, E, I, M, Q, U)
MGSHHHHHHSNDPMAKVQVNNVVVLDNPSPFYNPFQFEITFECIEDLSEDLEWKIIYVGS
AESEEYDQVLDSVLVGPVPAGRHMFVFQADAPNPGLIPDADAVGVTVVLITCTYRGQEFI
RVGYYVNNEYTETELRENPPVKPDFSKLQRNILASNPRVTRFHINWEDNTEKLEDAESSN
PNLQSLLS

Sequence of entity 2 (B, F, J, N, R, V), FASTA

>5C3I_2 Histone H3.1 (chains B, F, J, N, R, V)
MARTKQTARKSTGGKAPRKQLATKAARKSAPATGGVKKPHRYRPGTVALREIRRYQKSTE
LLIRKLPFQRLVREIAQDFKTDLRFQSSAVMALQEACEAYLVGLFEDTNLCAIHAKRVTI
MPKDIQLARRIRGERA

Sequence of entity 3 (C, G, K, O, S, W), FASTA

>5C3I_3 Histone H4 (chains C, G, K, O, S, W)
MSGRGKGGKGLGKGGAKRHRKVLRDNIQGITKPAIRRLARRGGVKRISGLIYEETRGVLK
VFLENVIRDAVTYTEHAKRKTVTAMDVVYALKRQGRTLYGFGG

Sequence of entity 4 (D, H, L, P, T, X), FASTA

>5C3I_4 DNA replication licensing factor MCM2,MCM2 (chains D, H, L, P, T, X)
SLEEEEDGEELIGDGMERDYRAIPELDAYEAEGLALDDEDVEELTASQREAAERAMRQRD
REAXXXXXXXXXXXXXXXXXXXXXXXXXXXXXX

Primary citation

Structure of the quaternary complex of histone H3-H4 heterodimer with chaperone ASF1 and the replicative helicase subunit MCM2. Wang, H., Wang, M., Yang, N. et al. Protein Cell (2015) 6:693-697. DOI 10.1007/s13238-015-0190-0 · 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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