Research workbench
Histone fold heterodimer of the chromatin accessibility complex
Analyse Histone fold heterodimer of the chromatin accessibility complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2BYK
- Type
- protein
- Length
- 319 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Chrac-16; Chrac-14
- UniProt
- Q9V452, Q9V444
- Ligands
- SO4
- Pockets
- 2 · best druggability 0.66
Structure
x-ray diffraction · 4 distinct chains · 65% helix, 3% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Chrac-16 | protein | 72 | 54% helix, 3% strand | Q9V452 |
| B | Chrac-14 | protein | 89 | 70% helix, 2% strand | Q9V444 |
| C | Chrac-16 | protein | 66 | 65% helix, 3% strand | Q9V452 |
| D | Chrac-14 | protein | 92 | 68% helix, 2% strand | Q9V444 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 3 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 291 | 0.66 | 0.82 | 46 | empty |
| 2 | 290 | 0.57 | 0.77 | 42 | empty |
Interfaces
6 interfaces between chains.
- C–D · 1845 Ų buried · 9 hydrogen bonds · protein-protein
- A–B · 1762 Ų buried · 9 hydrogen bonds · protein-protein
- A–C · 525 Ų buried · 8 hydrogen bonds · protein-protein
- B–D · 447 Ų buried · 3 hydrogen bonds · protein-protein
- A–D · 426 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 2BYK · Histone fold heterodimer of the Chromatin Accessibility Complex · the same entry in another collection · chain D against D, TM-score 1.00
- Q9V444 · AlphaFold monomer V2.0 prediction for DNA polymerase epsilon subunit 3 (Q9V444) · a predicted model of the same protein · chain B against A, TM-score 0.98
- Q9V452 · AlphaFold monomer V2.0 prediction for chromatin accessibility complex 16KD protein… · a predicted model of the same protein · chain C against A, TM-score 0.89
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt Q9V452
- Every structure of UniProt Q9V444
- Elsewhere: RCSB PDB 2BYK · PDBe 2BYK · UniProt Q9V452 · UniProt Q9V444
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