Research workbench
Human menin in complex with mll peptide
Analyse Human menin in complex with mll peptide in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4GQ6
- Type
- protein
- Length
- 479 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Menin; Histone-lysine N-methyltransferase mll
- EC
- 2.1.1.43
- UniProt
- O00255, Q03164
- Ligands
- SO4
- Pockets
- 4 · best druggability 0.73
Structure
x-ray diffraction · 2 distinct chains · 56% helix, 6% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Menin | protein | 467 | 57% helix, 6% strand | O00255 |
| B | Histone-lysine N-methyltransferase mll (EC 2.1.1.43) | protein | 12 | 0% helix, 8% strand | Q03164 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 3 copies · chains A
- 1PE · Pentaethylene glycol · additive · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 696 | 0.73 | 0.79 | 61 | empty |
| 2 | 92 | 0.37 | 0.76 | 20 | empty |
| 3 | 55 | 0.31 | 0.76 | 14 | empty |
| 4 | 53 | 0.31 | 0.77 | 14 | SO4 |
Interfaces
1 interface between chains.
- A–B · 834 Ų buried · 9 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 4GQ6 · PDBe 4GQ6 · UniProt O00255 · UniProt Q03164
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