6ZUF: Urea-based Foldamer Inhibitor chimera C2

Name: PDB 6ZUF: Urea-based Foldamer Inhibitor chimera C2 in complex with ASF1 Histone chaperone
Published: 2021-06-09
License: https://creativecommons.org/publicdomain/zero/1.0/
Keywords: chaperone

Urea-based Foldamer Inhibitor chimera C2 in complex with ASF1 Histone chaperone. Determined by X-ray diffraction at 1.8 Å resolution. Released 9 Jun 2021.

Method: X-ray diffraction
Resolution: 1.8 Å
Organism: Homo sapiens
Chains: 4
Atoms: 2,933
Mol. weight: 39.73 kDa
Released: 9 Jun 2021

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

Secondary structure: helices and β-sheets

6ZUF contains 17 α-helices and 24 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: 7 helices, 12 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	34	1	3
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	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: 8 helices, 12 β-strands

Element	Residues	Length	Sheet
β-strand	4-12	9	4
β-strand	16-17	2	5
α-helix	21	1
β-strand	22-30	9	4
β-strand	34	1	6
β-strand	38-45	8	5
α-helix	51-53	3
β-strand	54-62	9	5
β-strand	65	1	6
α-helix	66	1
β-strand	68-76	9	4
α-helix	77-79	3
α-helix	81-83	3
α-helix	86-89	4
β-strand	91-101	11	5
β-strand	104-117	14	5
α-helix	120-124	5
α-helix	132-134	3
β-strand	135-139	5	5
β-strand	145-148	4	5

Chains C and D: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	3-6	4

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Histone chaperone ASF1A	A, B	protein	158	Homo sapiens	Q9Y294 (AlphaFold model)
C2 foldamer/peptide hybrid inhibitor of histone chaperone ASF1	C, D	protein	9	Homo sapiens

Sequence of entity 1 (A, B), FASTA

>6ZUF_1 Histone chaperone ASF1A (chains A, B)
GAMAKVQVNNVVVLDNPSPFYNPFQFEITFECIEDLSEDLEWKIIYVGSAESEEYDQVLD
SVLVGPVPAGRHMFVFQADAPNPGLIPDADAVGVTVVLITCTYRGQEFIRVGYYVNNEYT
ETELRENPPVKPDFSKLQRNILASNPRVTRFHINWEDN

Sequence of entity 2 (C, D), FASTA

>6ZUF_2 C2 foldamer/peptide hybrid inhibitor of histone chaperone ASF1 (chains C, D)
EKXXXQRIA

Primary citation

Optimal anchoring of a foldamer inhibitor of ASF1 histone chaperone through backbone plasticity. Mbianda, J., Bakail, M., Andre, C. et al. Sci Adv (2021) 7. DOI 10.1126/sciadv.abd9153 · 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
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…
2IO5 2.7 Å, Crystal structure of the CIA- histone H3-H4 complex

Browse structure collections

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