MolNFT v1 · #118547 · protein
The crystal structure of MLL1 set domain with N3816I/Q3867L mutation
5F5E · Histone-lysine N-methyltransferase 2A: “The crystal structure of MLL1 set domain with N3816I/Q3867L mutation”. X-ray diffraction, 2 ligands (SAH, ZN), 1 pocket (best druggability 0.48). MolNFT v1 #118547 on GenesisL1: 3D structure…
- PDB
- 5F5E
- Type
- protein
- Length
- 148 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Histone-lysine N-methyltransferase 2A
- EC
- 2.1.1.43
- UniProt
- Q03164
- Ligands
- SAH, ZN
- Pockets
- 1 · best druggability 0.48
Structure
x-ray diffraction · 1 distinct chain · 22% helix, 34% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Histone-lysine N-methyltransferase 2A (EC 2.1.1.43) | protein | 148 | 22% helix, 34% strand | Q03164 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 189 | 0.48 | 0.75 | 28 | SAH |
Compared structures
- 5F5E · The Crystal Structure of MLL1 SET domain with N3816I/Q3867L mutation · 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 Q03164
- Elsewhere: RCSB PDB 5F5E · PDBe 5F5E · UniProt Q03164
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.