Research workbench
X-ray structure of WDR5-MLL1 win motif peptide binary complex
Analyse X-ray structure of WDR5-MLL1 win motif peptide binary complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4ESG
- Type
- protein
- Length
- 640 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Wd repeat-containing protein 5; Histone-lysine N-methyltransferase mll
- EC
- 2.1.1.43
- UniProt
- P61964, Q03164
- Pockets
- 3 · best druggability 0.74
Structure
x-ray diffraction · 2 distinct chains · 1% helix, 49% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Wd repeat-containing protein 5 | protein | 304 | 0% helix, 51% strand | P61964 |
| C, D | Histone-lysine N-methyltransferase mll (EC 2.1.1.43) | protein | 16 | 19% helix, 0% strand | Q03164 |
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 | 456 | 0.74 | 0.83 | 43 | empty |
| 2 | 446 | 0.73 | 0.82 | 44 | empty |
| 3 | 419 | 0.58 | 0.75 | 55 | empty |
Interfaces
3 interfaces between chains.
- A–D · 699 Ų buried · 11 hydrogen bonds · protein-protein
- B–C · 697 Ų buried · 11 hydrogen bonds · protein-protein
- A–B · 292 Ų buried · 6 hydrogen bonds · protein-protein
Compared structures
- 4ESG · X-ray structure of WDR5-MLL1 Win motif peptide binary 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
- Every structure of UniProt Q03164
- Elsewhere: RCSB PDB 4ESG · PDBe 4ESG · UniProt P61964 · UniProt Q03164
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