Research workbench
Crystal structure of MRG15-ASH1L histone methyltransferase complex
Analyse Crystal structure of MRG15-ASH1L histone methyltransferase complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6AGO
- Type
- protein
- Length
- 791 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Histone-lysine N-methyltransferase ASH1L; Mortality factor 4 like 1
- EC
- 2.1.1.43
- UniProt
- Q9NR48, A5D8W6
- Ligands
- SAM, ZN
- Pockets
- 10 · best druggability 0.83
Structure
x-ray diffraction · 4 distinct chains · 31% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Histone-lysine N-methyltransferase ASH1L (EC 2.1.1.43) | protein | 242 | 13% helix, 23% strand | Q9NR48 |
| B | Histone-lysine N-methyltransferase ASH1L (EC 2.1.1.43) | protein | 224 | 12% helix, 23% strand | Q9NR48 |
| C | Mortality factor 4 like 1 | protein | 167 | 58% helix, 4% strand | A5D8W6 |
| D | Mortality factor 4 like 1 | protein | 158 | 58% helix, 4% strand | A5D8W6 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
10 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1181 | 0.83 | 0.84 | 100 | empty |
| 2 | 153 | 0.69 | 0.88 | 31 | empty |
| 3 | 500 | 0.68 | 0.79 | 38 | empty |
| 4 | 202 | 0.65 | 0.84 | 32 | empty |
| 5 | 68 | 0.55 | 0.88 | 24 | empty |
Interfaces
6 interfaces between chains.
- B–D · 1673 Ų buried · 22 hydrogen bonds · protein-protein
- A–C · 1650 Ų buried · 24 hydrogen bonds · protein-protein
- A–B · 1065 Ų buried · 20 hydrogen bonds · protein-protein
- B–C · 382 Ų buried · 3 hydrogen bonds · protein-protein
- A–D · 342 Ų buried · 2 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 covalent (covalent ligand).
Compared structures
- 6AGO · Crystal structure of MRG15-ASH1L Histone methyltransferase complex · 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
- Every structure of UniProt A5D8W6
- Elsewhere: RCSB PDB 6AGO · PDBe 6AGO · UniProt Q9NR48 · UniProt A5D8W6
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