Research workbench
Histone H3 recognition and presentation by the WDR5 module of the MLL1 complex
Analyse Histone H3 recognition and presentation by the WDR5 module of the MLL1 complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2H6K
- Type
- protein
- Length
- 628 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Wd-repeat protein 5; Histone H3 K4-me 9-residue peptide
- UniProt
- P61964
- Pockets
- 3 · best druggability 0.84
Structure
x-ray diffraction · 4 distinct chains · 0% helix, 50% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Wd-repeat protein 5 | protein | 305 | 0% helix, 52% strand | P61964 |
| B | Wd-repeat protein 5 | protein | 306 | 0% helix, 51% strand | P61964 |
| C | Histone H3 K4-me 9-residue peptide | protein | 9 | 0% helix, 0% strand | — |
| D | Histone H3 K4-me 9-residue peptide | protein | 8 | 0% helix, 0% strand | — |
Pockets
3 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 834 | 0.84 | 0.86 | 77 | empty |
| 2 | 502 | 0.73 | 0.82 | 44 | empty |
| 3 | 177 | 0.55 | 0.80 | 27 | empty |
Interfaces
3 interfaces between chains.
- A–C · 713 Ų buried · 13 hydrogen bonds · protein-protein
- B–D · 691 Ų buried · 13 hydrogen bonds · protein-protein
- A–B · 487 Ų buried · 4 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 modified (methylation).
Compared structures
- 2H6K · Histone H3 recognition and presentation by the WDR5 module of the MLL1 complex · the same entry in another collection · chain A against A, TM-score 1.00
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 P61964
- Elsewhere: RCSB PDB 2H6K · PDBe 2H6K · UniProt P61964
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