Research workbench
Crystal structure of WDR5 in complex with the WDR5-interacting motif of MLL2
Analyse Crystal structure of WDR5 in complex with the WDR5-interacting motif of MLL2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3UVK
- Type
- protein
- Length
- 310 residues
- Chains
- 2
- 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
- Ligands
- SO4
- Pockets
- 2 · best druggability 0.75
Structure
x-ray diffraction · 2 distinct chains · 1% helix, 51% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Wd repeat-containing protein 5 | protein | 299 | 0% helix, 53% strand | P61964 |
| B | Histone-lysine N-methyltransferase MLL2 (EC 2.1.1.43) | protein | 11 | 27% helix, 0% strand | O14686 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · chains A
- BTB · 2-[bis-(2-hydroxy-ethyl)-amino]-2-hydroxymethyl-propane-1,3-diol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
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 | 455 | 0.75 | 0.84 | 46 | BTB, SO4 |
| 2 | 86 | 0.37 | 0.75 | 15 | empty |
Interfaces
1 interface between chains.
- A–B · 644 Ų buried · 11 hydrogen bonds · protein-protein
Compared structures
- 3UVK · Crystal structure of WDR5 in complex with the WDR5-interacting motif of MLL2 · 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 3UVK · PDBe 3UVK · UniProt P61964 · UniProt O14686
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