8BV1: Peptide inhibitor P4
Peptide inhibitor P4 in complex with ASF1 histone chaperone. Determined by X-ray diffraction at 2.83 Å resolution. Released 5 Jul 2023.
- Method
- X-ray diffraction
- Resolution
- 2.83 Å
- Organisms
- Homo sapiens, synthetic construct
- Chains
- 12
- Atoms
- 8,282
- Mol. weight
- 117.4 kDa
- Released
- 5 Jul 2023
Explore 8BV1 in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
8BV1 contains 45 α-helices and 70 β-strands across 12 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, 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 |
| α-helix | 37 | 1 | |
| 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: 6 helices, 10 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 4-11 | 8 | 4 |
| β-strand | 16-17 | 2 | 5 |
| α-helix | 21 | 1 | |
| β-strand | 22-30 | 9 | 4 |
| β-strand | 38-45 | 8 | 5 |
| α-helix | 51-53 | 3 | |
| β-strand | 54-62 | 9 | 5 |
| 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 | |
| β-strand | 135-139 | 5 | 5 |
| β-strand | 145-148 | 4 | 5 |
Chain C: 6 helices, 12 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 4-11 | 8 | 6 |
| β-strand | 16-17 | 2 | 7 |
| α-helix | 21 | 1 | |
| β-strand | 22-30 | 9 | 6 |
| β-strand | 34 | 1 | 8 |
| β-strand | 38-45 | 8 | 7 |
| α-helix | 51-53 | 3 | |
| β-strand | 54-62 | 9 | 7 |
| β-strand | 65 | 1 | 8 |
| β-strand | 68-76 | 9 | 6 |
| α-helix | 77-79 | 3 | |
| α-helix | 81-83 | 3 | |
| α-helix | 86-89 | 4 | |
| β-strand | 91-101 | 11 | 7 |
| β-strand | 104-117 | 14 | 7 |
| α-helix | 120-124 | 5 | |
| β-strand | 135-139 | 5 | 7 |
| β-strand | 145-148 | 4 | 7 |
Chains D and E: 6 helices, 12 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 4-12 | 9 | 9 |
| β-strand | 16-17 | 2 | 10 |
| α-helix | 21 | 1 | |
| β-strand | 22-30 | 9 | 9 |
| β-strand | 34 | 1 | 11 |
| β-strand | 38-45 | 8 | 10 |
| α-helix | 51-53 | 3 | |
| β-strand | 54-62 | 9 | 10 |
| β-strand | 65 | 1 | 11 |
| β-strand | 68-76 | 9 | 9 |
| α-helix | 77-79 | 3 | |
| α-helix | 81-83 | 3 | |
| α-helix | 86-89 | 4 | |
| β-strand | 91-101 | 11 | 10 |
| β-strand | 104-117 | 14 | 10 |
| α-helix | 120-124 | 5 | |
| β-strand | 135-139 | 5 | 10 |
| β-strand | 145-148 | 4 | 10 |
Chain F: 7 helices, 12 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 4-12 | 9 | 15 |
| β-strand | 16-17 | 2 | 16 |
| α-helix | 21 | 1 | |
| β-strand | 22-30 | 9 | 15 |
| β-strand | 34 | 1 | 17 |
| β-strand | 38-45 | 8 | 16 |
| α-helix | 51-53 | 3 | |
| β-strand | 54-62 | 9 | 16 |
| β-strand | 65 | 1 | 17 |
| β-strand | 68-76 | 9 | 15 |
| α-helix | 77-79 | 3 | |
| α-helix | 81-83 | 3 | |
| α-helix | 86-89 | 4 | |
| β-strand | 91-101 | 11 | 16 |
| β-strand | 104-117 | 14 | 16 |
| α-helix | 120-124 | 5 | |
| α-helix | 132-134 | 3 | |
| β-strand | 135-139 | 5 | 16 |
| β-strand | 145-148 | 4 | 16 |
Chains G, H, I, K, L and N: 1 helix, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 3-11 | 9 | |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Histone chaperone ASF1A | A, B, C, D, E, F | protein | 158 | Homo sapiens | Q9Y294 (AlphaFold model) |
| P4 peptide inhibitor of histone chaperone ASF1 | G, H, I, K, L, N | protein | 13 | synthetic construct | |
Sequence of entity 1 (A, B, C, D, E, F), FASTA
>8BV1_1 Histone chaperone ASF1A (chains A, B, C, D, E, F)
GAMAKVQVNNVVVLDNPSPFYNPFQFEITFECIEDLSEDLEWKIIYVGSAESEEYDQVLD
SVLVGPVPAGRHMFVFQADAPNPGLIPDADAVGVTVVLITCTYRGQEFIRVGYYVNNEYT
ETELRENPPVKPDFSKLQRNILASNPRVTRFHINWEDN
Sequence of entity 2 (G, H, I, K, L, N), FASTA
>8BV1_2 P4 peptide inhibitor of histone chaperone ASF1 (chains G, H, I, K, L, N)
XEKAARLARRIAX
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
- 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
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