Research workbench
Crystal structure of human menin in apo form
Analyse Crystal structure of human menin in apo form in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7O9T
- Type
- protein
- Length
- 457 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Menin
- UniProt
- A0A024R5E3
- Pockets
- 3 · best druggability 0.60
Structure
x-ray diffraction · 1 distinct chain · 58% helix, 6% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Menin | protein | 457 | 58% helix, 6% strand | A0A024R5E3 |
Ligands and binding sites
- EDO · 1,2-ethanediol · additive · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 393 | 0.60 | 0.76 | 45 | EDO |
| 2 | 51 | 0.54 | 0.89 | 24 | empty |
| 3 | 84 | 0.32 | 0.73 | 14 | EDO |
Compared structures
- 7O9T · Crystal structure of Human Menin in apo form · 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 A0A024R5E3
- Elsewhere: RCSB PDB 7O9T · PDBe 7O9T · UniProt A0A024R5E3
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