8CJ2: Urea-based foldamer inhibitor c3u_5 chimera

Name: PDB 8CJ2: Urea-based foldamer inhibitor c3u_5 chimera in complex with ASF1 histone chaperone
Published: 2023-07-05
License: https://creativecommons.org/publicdomain/zero/1.0/
Keywords: chaperone

Urea-based foldamer inhibitor c3u_5 chimera in complex with ASF1 histone chaperone. Determined by X-ray diffraction at 2.13 Å resolution. Released 5 Jul 2023.

Method: X-ray diffraction
Resolution: 2.13 Å
Organism: Homo sapiens
Chains: 8
Atoms: 5,777
Mol. weight: 78.17 kDa
Released: 5 Jul 2023

Explore 8CJ2 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

8CJ2 contains 32 α-helices and 40 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.

Chains A, C and D: 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: 7 helices, 10 β-strands

Element	Residues	Length	Sheet
β-strand	4-11	8	3
β-strand	16-17	2	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	86-88	3
β-strand	91-101	11	4
β-strand	104-117	14	4
α-helix	120-124	5
α-helix	132-134	3
β-strand	135-139	5	4
β-strand	145-148	4	4

Chains E, F and G: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	5-7	3

Chain H: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	5-8	4

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Histone chaperone ASF1A	A, B, C, D	protein	156	Homo sapiens	Q9Y294 (AlphaFold model)
c3u_5 chimera inhibitor of histone chaperone ASF1	E, F, G, H	protein	11	Homo sapiens

Sequence of entity 1 (A, B, C, D), FASTA

>8CJ2_1 Histone chaperone ASF1A (chains A, B, C, D)
MAKVQVNNVVVLDNPSPFYNPFQFEITFECIEDLSEDLEWKIIYVGSAESEEYDQVLDSV
LVGPVPAGRHMFVFQADAPNPGLIPDADAVGVTVVLITCTYRGQEFIRVGYYVNNEYTET
ELRENPPVKPDFSKLQRNILASNPRVTRFHINWEDN

Sequence of entity 2 (E, F, G, H), FASTA

>8CJ2_2 c3u_5 chimera inhibitor of histone chaperone ASF1 (chains E, F, G, H)
XEKAAXXQRIX

Primary citation

Unexpected binding modes of inhibitors to the histone chaperone ASF1 revealed by a foldamer scanning approach. Perrin, M.E., Li, B., Mbianda, J. et al. Chem Commun (Camb) (2023) 59:8696-8699. DOI 10.1039/d3cc01891a · 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
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

Browse structure collections

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