Research workbench
ASH1L set domain K2264L mutant in complex with S-adenosyl methionine (SAM)
Analyse ASH1L set domain K2264L mutant in complex with S-adenosyl methionine (SAM) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4YPU
- Type
- protein
- Length
- 404 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 0.79
Structure
x-ray diffraction · 2 distinct chains · 10% helix, 30% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Histone-lysine N-methyltransferase ASH1L (EC 2.1.1.43) | protein | 214 | 12% helix, 30% strand | Q9NR48 |
| B | Histone-lysine N-methyltransferase ASH1L (EC 2.1.1.43) | protein | 190 | 8% helix, 31% 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 | 776 | 0.79 | 0.83 | 60 | empty |
| 2 | 190 | 0.67 | 0.86 | 33 | SAM |
| 3 | 285 | 0.62 | 0.80 | 32 | SAM |
| 4 | 131 | 0.48 | 0.79 | 25 | empty |
| 5 | 110 | 0.39 | 0.75 | 15 | empty |
Interfaces
1 interface between chains.
- A–B · 557 Ų buried · 1 hydrogen bond · protein-protein
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 4YPU · ASH1L SET domain K2264L mutant in complex with S-adenosyl methionine (SAM) · 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 Q9NR48
- Elsewhere: RCSB PDB 4YPU · PDBe 4YPU · UniProt Q9NR48
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