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Crystal structure of human menin in complex with MLL1
Analyse Crystal structure of human menin in complex with MLL1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3U85
- Type
- protein
- Length
- 493 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Menin; Histone-lysine N-methyltransferase 2A
- EC
- 2.1.1.43
- UniProt
- O00255, Q03164
- Pockets
- 5 · best druggability 0.67
Structure
x-ray diffraction · 2 distinct chains · 52% helix, 7% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Menin | protein | 484 | 53% helix, 7% strand | O00255 |
| B | Histone-lysine N-methyltransferase 2A (EC 2.1.1.43) | protein | 9 | 0% helix, 0% strand | Q03164 |
Pockets
5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 454 | 0.67 | 0.79 | 49 | empty |
| 2 | 169 | 0.53 | 0.79 | 19 | empty |
| 3 | 72 | 0.40 | 0.79 | 17 | empty |
| 4 | 68 | 0.35 | 0.77 | 17 | empty |
| 5 | 59 | 0.27 | 0.74 | 16 | empty |
Interfaces
1 interface between chains.
- A–B · 758 Ų buried · 7 hydrogen bonds · protein-protein
Compared structures
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 O00255
- Every structure of UniProt Q03164
- Elsewhere: RCSB PDB 3U85 · PDBe 3U85 · UniProt O00255 · UniProt Q03164
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