Research workbench
Crystal structure of AF9 yeats domain Y78W mutant in complex with histone H3K9CR
Analyse Crystal structure of AF9 yeats domain Y78W mutant in complex with histone H3K9CR in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6MIM
- Type
- protein
- Length
- 286 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein af-9; Histone H3K9CR
- UniProt
- P42568
- Pockets
- 3 · best druggability 0.66
Structure
x-ray diffraction · 2 distinct chains · 9% helix, 50% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | Protein af-9 | protein | 137 | 9% helix, 51% strand | P42568 |
| B, D | Histone H3K9CR | protein | 6 | 0% helix, 17% strand | — |
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 545 | 0.66 | 0.77 | 48 | empty |
| 2 | 97 | 0.37 | 0.75 | 17 | empty |
| 3 | 52 | 0.30 | 0.76 | 15 | empty |
Interfaces
4 interfaces between chains.
- C–D · 546 Ų buried · 7 hydrogen bonds · protein-protein
- A–B · 543 Ų buried · 9 hydrogen bonds · protein-protein
- A–C · 120 Ų buried · 0 hydrogen bonds · protein-protein
- A–D · 93 Ų buried · 1 hydrogen bond · protein-protein
Modifications
Observed in the structure: 2 modified (nonstandard).
Compared structures
- 6MIM · Crystal structure of AF9 YEATS domain Y78W mutant in complex with histone H3K9cr · the same entry in another collection · chain A against A, TM-score 1.00
- P42568 · AlphaFold monomer V2.0 prediction for protein af-9 (P42568) · a predicted model of the same protein · chain C against A, TM-score 0.99
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 P42568
- Elsewhere: RCSB PDB 6MIM · PDBe 6MIM · UniProt P42568
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