Research workbench
Structural basis for the specific recognition of methylated histone H3 lysine 4 by the wd-40 protein WDR5
Analyse Structural basis for the specific recognition of methylated histone H3 lysine 4… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2G9A
- Type
- protein
- Length
- 315 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Wd-repeat protein 5; Histone H3
- UniProt
- P61964
- Pockets
- 2 · best druggability 0.75
Structure
x-ray diffraction · 2 distinct chains · 0% helix, 50% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Wd-repeat protein 5 | protein | 310 | 0% helix, 50% strand | P61964 |
| B | Histone H3 | protein | 5 | 0% helix, 0% strand | — |
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 522 | 0.75 | 0.83 | 51 | empty |
| 2 | 63 | 0.38 | 0.79 | 17 | empty |
Interfaces
1 interface between chains.
- A–B · 484 Ų buried · 7 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 modified (methylation).
Compared structures
- 2G9A · Structural basis for the specific recognition of methylated histone H3 lysine 4 by the… · 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 2G9A · PDBe 2G9A · UniProt P61964
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