6F0F: Crystal structure ASF1-ip2_s

Name: PDB 6F0F: Crystal structure ASF1-ip2_s
Published: 2019-06-12
License: https://creativecommons.org/publicdomain/zero/1.0/
Keywords: chaperone

Crystal structure ASF1-ip2_s. Determined by X-ray diffraction at 2.0 Å resolution. Released 12 Jun 2019.

Method: X-ray diffraction
Resolution: 2.0 Å
Organism: Homo sapiens
Chains: 2
Atoms: 1,804
Mol. weight: 20.89 kDa
Released: 12 Jun 2019

Explore 6F0F in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6F0F contains 9 α-helices and 11 β-strands across 2 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	54-62	9	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	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: 2 helices, 1 β-strand

Element	Residues	Length	Sheet
α-helix	221-231	11
α-helix	235-236	2
β-strand	237-239	3	2

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Histone chaperone ASF1A	A	protein	158	Homo sapiens	Q9Y294 (AlphaFold model)
ip2_s	B	protein	29	Homo sapiens

Sequence of entity 1 (A), FASTA

>6F0F_1 Histone chaperone ASF1A (chains A)
GAMAKVQVNNVVVLDNPSPFYNPFQFEITFECIEDLSEDLEWKIIYVGSAESEEYDQVLD
SVLVGPVPAGRHMFVFQADAPNPGLIPDADAVGVTVVLITCTYRGQEFIRVGYYVNNEYT
ETELRENPPVKPDFSKLQRNILASNPRVTRFHINWEDN

Sequence of entity 2 (B), FASTA

>6F0F_2 ip2_s (chains B)
GAMGTLTPKEAELARRIRGAGGRTLNGFG

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
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…
2IO5 2.7 Å, Crystal structure of the CIA- histone H3-H4 complex

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