6F0G: Crystal structure ASF1-ip3

Name: PDB 6F0G: Crystal structure ASF1-ip3
Published: 2019-06-12
License: https://creativecommons.org/publicdomain/zero/1.0/
Keywords: chaperone

Crystal structure ASF1-ip3. Determined by X-ray diffraction at 2.3 Å resolution. Released 12 Jun 2019.

Method: X-ray diffraction
Resolution: 2.3 Å
Organism: Homo sapiens
Chains: 4
Atoms: 3,046
Mol. weight: 41.61 kDa
Released: 12 Jun 2019

Explore 6F0G in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6F0G contains 18 α-helices and 22 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: 8 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	38-44	7	2
α-helix	51-53	3
β-strand	55-62	8	2
α-helix	65-66	2
β-strand	68-76	9	1
α-helix	77-79	3
α-helix	81-83	3
α-helix	86-89	4
β-strand	91-101	11	2
β-strand	105-117	13	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: 8 helices, 10 β-strands

Element	Residues	Length	Sheet
β-strand	4-12	9	3
β-strand	16-17	2	4
α-helix	21	1
β-strand	22-30	9	3
β-strand	38-44	7	4
α-helix	51-53	3
β-strand	55-62	8	4
α-helix	65-66	2
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	105-117	13	4
α-helix	120-124	5
α-helix	132-134	3
β-strand	135-139	5	4
β-strand	145-148	4	4

Chains C and D: 1 helix, 1 β-strand

Element	Residues	Length	Sheet
α-helix	220-231	12
β-strand	236-239	4	2

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Histone chaperone ASF1A	A, B	protein	158	Homo sapiens	Q9Y294 (AlphaFold model)
ip3	C, D	protein	26	Homo sapiens

Sequence of entity 1 (A, B), FASTA

>6F0G_1 Histone chaperone ASF1A (chains A, B)
GAMAKVQVNNVVVLDNPSPFYNPFQFEITFECIEDLSEDLEWKIIYVGSAESEEYDQVLD
SVLVGPVPAGRHMFVFQADAPNPGLIPDADAVGVTVVLITCTYRGQEFIRVGYYVNNEYT
ETELRENPPVKPDFSKLQRNILASNPRVTRFHINWEDN

Sequence of entity 2 (C, D), FASTA

>6F0G_2 ip3 (chains C, D)
ASTERKWAELARRIRGAGGVTLNGFG

Primary citation

Design on a Rational Basis of High-Affinity Peptides Inhibiting the Histone Chaperone ASF1. Bakail, M., Gaubert, A., Andreani, J. et al. Cell Chem Biol (2019) 26:1573-1585.e10. DOI 10.1016/j.chembiol.2019.09.002 · 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
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

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