7V6Q: SNASP-ASF1A-H3.1-H4 complex

Name: PDB 7V6Q: Crystal structure of sNASP-ASF1A-H3.1-H4 complex
Published: 2021-12-29
License: https://creativecommons.org/publicdomain/zero/1.0/
Keywords: chaperone

Crystal structure of sNASP-ASF1A-H3.1-H4 complex. Determined by X-ray diffraction at 3.0 Å resolution. Released 29 Dec 2021.

Method: X-ray diffraction
Resolution: 3.0 Å
Organism: Homo sapiens
Chains: 8
Atoms: 8,594
Mol. weight: 153.97 kDa
Released: 29 Dec 2021

Explore 7V6Q in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

7V6Q contains 53 α-helices and 28 β-strands across 8 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, 9 β-strands

Element	Residues	Length	Sheet
β-strand	4-12	9	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	54-62	9	2
α-helix	65-66	2
β-strand	68-76	9	1
α-helix	77-79	3
α-helix	81-83	3
α-helix	86-88	3
β-strand	91-101	11	2
β-strand	104-117	14	2
α-helix	120-124	5
β-strand	135-148	14	2

Chain B: 8 helices, 2 β-strands

Element	Residues	Length	Sheet
α-helix	45-48	4
α-helix	52-56	5
α-helix	64-77	14
α-helix	82	1
β-strand	83-84	2	3
α-helix	85	1
α-helix	86-112	27
α-helix	113-115	3
β-strand	119	1	4
α-helix	121-130	10

Chain C: 3 helices, 3 β-strands

Element	Residues	Length	Sheet
α-helix	31-41	11
β-strand	46	1	4
α-helix	49-75	27
β-strand	80-81	2	3
α-helix	83-91	9
β-strand	95-97	3	2

Chain D: 10 helices, 0 β-strands

Element	Residues	Length
α-helix	41-56	16
α-helix	59-77	19
α-helix	82-84	3
α-helix	85-101	17
α-helix	175-191	17
α-helix	196-215	20
α-helix	219-236	18
α-helix	242-257	16
α-helix	261-288	28
α-helix	295-318	24

Chain E: 6 helices, 9 β-strands

Element	Residues	Length	Sheet
β-strand	4-12	9	5
β-strand	16-17	2	6
α-helix	21	1
β-strand	22-30	9	5
β-strand	38-45	8	6
α-helix	51-53	3
β-strand	54-62	9	6
β-strand	68-76	9	5
α-helix	77-79	3
α-helix	81-83	3
α-helix	86-88	3
β-strand	91-101	11	6
β-strand	104-117	14	6
α-helix	120-124	5
β-strand	135-148	14	6

Chain F: 6 helices, 2 β-strands

Element	Residues	Length	Sheet
α-helix	45-48	4
α-helix	52-56	5
α-helix	64-78	15
β-strand	83-84	2	7
α-helix	86-112	27
α-helix	113-115	3
β-strand	118-119	2	8
α-helix	121-130	10

Chain G: 3 helices, 3 β-strands

Element	Residues	Length	Sheet
α-helix	31-41	11
β-strand	45-46	2	8
α-helix	50-76	27
β-strand	80-81	2	7
α-helix	83-91	9
β-strand	95-97	3	6

Chain H: 10 helices, 0 β-strands

Element	Residues	Length
α-helix	41-56	16
α-helix	59-77	19
α-helix	82-84	3
α-helix	85-101	17
α-helix	175-192	18
α-helix	196-215	20
α-helix	219-236	18
α-helix	242-257	16
α-helix	261-284	24
α-helix	299-318	20

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Histone chaperone ASF1A	A, E	protein	156	Homo sapiens	Q9Y294 (AlphaFold model)
Histone H3.1	B, F	protein	136	Homo sapiens	P68431 (AlphaFold model)
Histone H4	C, G	protein	102	Homo sapiens	P62805 (AlphaFold model)
Isoform 2 of Nuclear autoantigenic sperm protein	D, H	protein	283	Homo sapiens	P49321 (AlphaFold model)

Sequence of entity 1 (A, E), FASTA

>7V6Q_1 Histone chaperone ASF1A (chains A, E)
MAKVQVNNVVVLDNPSPFYNPFQFEITFECIEDLSEDLEWKIIYVGSAESEEYDQVLDSV
LVGPVPAGRHMFVFQADAPNPGLIPDADAVGVTVVLITCTYRGQEFIRVGYYVNNEYTET
ELRENPPVKPDFSKLQRNILASNPRVTRFHINWEDN

Sequence of entity 2 (B, F), FASTA

>7V6Q_2 Histone H3.1 (chains B, F)
MARTKQTARKSTGGKAPRKQLATKAARKSAPATGGVKKPHRYRPGTVALREIRRYQKSTE
LLIRKLPFQRLVREIAQDFKTDLRFQSSAVMALQEACEAYLVGLFEDTNLCAIHAKRVTI
MPKDIQLARRIRGERA

Sequence of entity 3 (C, G), FASTA

>7V6Q_3 Histone H4 (chains C, G)
MGRGKGGKGLGKGGAKRHRKVLRDNIQGITKPAIRRLARRGGVKRISGLIYEETRGVLKV
FLENVIRDAVTYTEHAKRKTVTAMDVVYALKRQGRTLYGFGG

Sequence of entity 4 (D, H), FASTA

>7V6Q_4 Isoform 2 of Nuclear autoantigenic sperm protein (chains D, H)
DPDSEAKKLLGLGQKHLVMGDIPAAVNAFQEAASLLGKKYGETANECGEAFFFYGKSLLE
LARMENGVLGNALEGVHVEEEEGEKTEDESLVENNDNIDETEGSEEDDKENDKTEEMPND
SVLENKSLQENEEEEIGNLELAWDMLDLAKIIFKRQETKEAQLYAAQAHLKLGEVSVESE
NYVQAVEEFQSCLNLQEQYLEAHDRLLAETHYQLGLAYGYNSQYDEAVAQFSKSIEVIEN
RMAVLNEQVKEAEGSSAEYKKEIEELKELLPEIREKIEDAKES

Primary citation

Distinct histone H3-H4 binding modes of sNASP reveal the basis for cooperation and competition of histone chaperones. Liu, C.P., Jin, W., Hu, J. et al. Genes Dev (2021) 35:1610-1624. DOI 10.1101/gad.349100.121 · 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…

Browse structure collections

About this viewer

MolViewer shows 7V6Q directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.