MolNFT v1 · #90731 · protein
X-ray structure of WDR5-MLL4 win motif peptide binary complex
4ERZ · Wd repeat-containing protein 5: “X-ray structure of WDR5-MLL4 win motif peptide binary complex”. X-ray diffraction, 7 pockets (best druggability 0.74). MolNFT v1 #90731 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 4ERZ
- Type
- protein
- Length
- 948 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 MLL4
- EC
- 2.1.1.43
- UniProt
- P61964, Q9UMN6
- Pockets
- 7 · 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, C | Wd repeat-containing protein 5 | protein | 304 | 0% helix, 51% strand | P61964 |
| D, E, F | Histone-lysine N-methyltransferase MLL4 (EC 2.1.1.43) | protein | 12 | 25% helix, 0% strand | Q9UMN6 |
Pockets
7 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 496 | 0.74 | 0.83 | 45 | empty |
| 2 | 492 | 0.73 | 0.82 | 46 | empty |
| 3 | 475 | 0.73 | 0.82 | 43 | empty |
| 4 | 847 | 0.69 | 0.75 | 79 | empty |
| 5 | 89 | 0.35 | 0.75 | 28 | empty |
Interfaces
5 interfaces between chains.
- C–D · 729 Ų buried · 10 hydrogen bonds · protein-protein
- B–F · 725 Ų buried · 10 hydrogen bonds · protein-protein
- A–E · 720 Ų buried · 10 hydrogen bonds · protein-protein
- A–B · 537 Ų buried · 7 hydrogen bonds · protein-protein
- A–C · 387 Ų buried · 7 hydrogen bonds · protein-protein
Compared structures
- 4ERZ · X-ray structure of WDR5-MLL4 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 Q9UMN6
- Elsewhere: RCSB PDB 4ERZ · PDBe 4ERZ · UniProt P61964 · UniProt Q9UMN6
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