MolNFT v1 · #111387 · protein
ASH1L set domain H2193F mutant in complex with S-adenosyl methionine (SAM)
4YPE · Histone-lysine N-methyltransferase ASH1L: “ASH1L set domain H2193F mutant in complex with S-adenosyl methionine (SAM)”. X-ray diffraction, 2 ligands (SAM, ZN), 5 pockets (best druggability 0.78). MolNFT v1 #111387 on GenesisL1: 3D…
- PDB
- 4YPE
- Type
- protein
- Length
- 419 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Histone-lysine N-methyltransferase ASH1L
- EC
- 2.1.1.43
- UniProt
- Q9NR48
- Ligands
- SAM, ZN
- Pockets
- 5 · best druggability 0.78
Structure
x-ray diffraction · 2 distinct chains · 11% helix, 30% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Histone-lysine N-methyltransferase ASH1L (EC 2.1.1.43) | protein | 217 | 12% helix, 30% strand | Q9NR48 |
| B | Histone-lysine N-methyltransferase ASH1L (EC 2.1.1.43) | protein | 202 | 10% helix, 30% strand | Q9NR48 |
Ligands and binding sites
- SAM · S-adenosylmethionine · ligand · 2 copies · chains A, B
- ZN · Zinc ion · metal · 6 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1109 | 0.78 | 0.80 | 78 | empty |
| 2 | 187 | 0.53 | 0.78 | 22 | SAM |
| 3 | 170 | 0.52 | 0.79 | 20 | SAM |
| 4 | 151 | 0.42 | 0.75 | 17 | empty |
| 5 | 82 | 0.35 | 0.75 | 12 | empty |
Interfaces
1 interface between chains.
- A–B · 581 Ų buried · 2 hydrogen bonds · protein-protein
Compared structures
- 4YPE · ASH1L SET domain H2193F mutant in complex with S-adenosyl methionine (SAM) · the same entry in another collection · chain B against B, 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 Q9NR48
- Elsewhere: RCSB PDB 4YPE · PDBe 4YPE · UniProt Q9NR48
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