Research workbench
X-ray structure of WDR5-MLL2 win motif peptide binary complex
Analyse X-ray structure of WDR5-MLL2 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
- 4ERQ
- Type
- protein
- Length
- 951 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Wd repeat-containing protein 5; Histone-lysine N-methyltransferase MLL2
- EC
- 2.1.1.43
- UniProt
- P61964, O14686
- Pockets
- 8 · best druggability 0.74
Structure
x-ray diffraction · 2 distinct chains · 0% helix, 49% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C | Wd repeat-containing protein 5 | protein | 304 | 0% helix, 51% strand | P61964 |
| D, E, F | Histone-lysine N-methyltransferase MLL2 (EC 2.1.1.43) | protein | 13 | 0% helix, 0% strand | O14686 |
Pockets
8 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 476 | 0.74 | 0.83 | 43 | empty |
| 2 | 466 | 0.74 | 0.83 | 44 | empty |
| 3 | 502 | 0.73 | 0.82 | 46 | empty |
| 4 | 510 | 0.66 | 0.78 | 54 | empty |
| 5 | 574 | 0.62 | 0.74 | 39 | empty |
Interfaces
6 interfaces between chains.
- C–F · 704 Ų buried · 9 hydrogen bonds · protein-protein
- A–D · 687 Ų buried · 8 hydrogen bonds · protein-protein
- B–E · 687 Ų buried · 9 hydrogen bonds · protein-protein
- A–B · 525 Ų buried · 6 hydrogen bonds · protein-protein
- A–C · 428 Ų buried · 7 hydrogen bonds · protein-protein
Compared structures
- 4ERQ · X-ray structure of WDR5-MLL2 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 O14686
- Elsewhere: RCSB PDB 4ERQ · PDBe 4ERQ · UniProt P61964 · UniProt O14686
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