2YGV: Histone chaperone ASF1
Conserved N-terminal domain of the yeast Histone Chaperone Asf1 in complex with the C-terminal fragment of Rad53. Determined by X-ray diffraction at 2.94 Å resolution. Released 15 Feb 2012.
- Method
- X-ray diffraction
- Resolution
- 2.94 Å
- Organism
- SACCHAROMYCES CEREVISIAE
- Chains
- 8
- Atoms
- 5,400
- Mol. weight
- 81.96 kDa
- Released
- 15 Feb 2012
Explore 2YGV in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
2YGV contains 18 α-helices and 48 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.
Chain A: 4 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 |
| β-strand | 55-62 | 8 | 2 |
| β-strand | 68-76 | 9 | 1 |
| α-helix | 81-83 | 3 | |
| β-strand | 92-101 | 10 | 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: 3 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 |
| β-strand | 55-62 | 8 | 4 |
| β-strand | 68-76 | 9 | 3 |
| α-helix | 77-80 | 4 | |
| β-strand | 92-101 | 10 | 4 |
| β-strand | 104-117 | 14 | 4 |
| α-helix | 132-134 | 3 | |
| β-strand | 135-139 | 5 | 4 |
| β-strand | 145-148 | 4 | 4 |
Chains C and D: 5 helices, 10 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 4-11 | 8 | 5 |
| β-strand | 16-17 | 2 | 6 |
| α-helix | 21 | 1 | |
| β-strand | 22-30 | 9 | 5 |
| β-strand | 38-45 | 8 | 6 |
| β-strand | 55-62 | 8 | 6 |
| β-strand | 68-76 | 9 | 5 |
| α-helix | 77-80 | 4 | |
| α-helix | 81-83 | 3 | |
| β-strand | 92-101 | 10 | 6 |
| β-strand | 104-117 | 14 | 6 |
| α-helix | 120-124 | 5 | |
| α-helix | 132-134 | 3 | |
| β-strand | 135-139 | 5 | 6 |
| β-strand | 145-148 | 4 | 6 |
Chain E: 1 helix, 3 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 163-165 | 3 | 2 |
| β-strand | 168-169 | 2 | 1 |
| α-helix | 170-172 | 3 | |
| β-strand | 179 | 1 | 7 |
Chain F: 0 helices, 2 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 164-165 | 2 | 4 |
| β-strand | 168-169 | 2 | 3 |
Chain G: 0 helices, 2 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 164-165 | 2 | 6 |
| β-strand | 179 | 1 | 5 |
Chain H: 0 helices, 1 β-strand
| Element | Residues | Length | Sheet |
|---|
| β-strand | 164-165 | 2 | 8 |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Histone chaperone ASF1 | A, B, C, D | protein | 158 | SACCHAROMYCES CEREVISIAE | P32447 (AlphaFold model) |
| Serine/threonine-protein kinase RAD53 | E, F, G, H | protein | 22 | SACCHAROMYCES CEREVISIAE | P22216 (AlphaFold model) |
Sequence of entity 1 (A, B, C, D), FASTA
>2YGV_1 HISTONE CHAPERONE ASF1 (chains A, B, C, D)
GAMSIVSLLGIKVLNNPAKFTDPYEFEITFECLESLKHDLEWKLTYVGSSRSLDHDQELD
SILVGPVPVGVNKFVFSADPPSAELIPASELVSVTVILLSCSYDGREFVRVGYYVNNEYD
EEELRENPPAKVQVDHIVRNILAEKPRVTRFNIVWDNE
Sequence of entity 2 (E, F, G, H), FASTA
>2YGV_2 SERINE/THREONINE-PROTEIN KINASE RAD53 (chains E, F, G, H)
SKKVKRAKLDQTSKGPENLQFS
Primary citation
Surprising Complexity of the Asf1 Histone Chaperone-Rad53 Kinase Interaction. Jiao, Y., Seeger, K., Lautrette, A. et al. Proc Natl Acad Sci U S A (2012) 109:2866. DOI 10.1073/PNAS.1106023109 · PubMed
Other PDB entries of the same protein (UniProt P32447 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 1ROC 1.5 Å, Crystal structure of the histone deposition protein Asf1
- 5UCB 1.52 Å, Structure of antigen-Fab complex with engineered switch residue region.
- 2HUE 1.7 Å, Structure of the H3-H4 chaperone Asf1 bound to histones H3 and H4
- 5UEK 1.7 Å, Structure of antigen-Fab 12E complex with Histone chaperone ASF1
- 5UEA 1.7 Å, Structure of antigen-Fab complex with Histone chaperone ASF1
- 6AYZ 2.1 Å, Crystal structure of Asf1-Fab 12E complex
- 2IDC 2.2 Å, Structure of the Histone H3-Asf1 Chaperone Interaction
- 4ZBJ 2.25 Å, UBN1 peptide bound to H3.3/H4/Asf1
- 4EO5 2.35 Å, Yeast Asf1 bound to H3/H4G94P mutant
- 5EII 2.44 Å, Structural determination of an protein complex of a Fab with increased solubility
- 6AZ2 2.48 Å, Crystal structure of Asf1-Fab 12E complex
- 4RRP 2.79 Å, Crystal Structure of the Fab complexed with antigen Asf1p, Northeast Structural Genomics…
Browse structure collections
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