Research workbench
Structure of the MLL4 set domain
Analyse Structure of the MLL4 set domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4Z4P
- Type
- protein
- Length
- 161 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Histone-lysine N-methyltransferase 2D
- EC
- 2.1.1.43
- UniProt
- O14686
- Ligands
- SAH, ZN
- Pockets
- 2 · best druggability 0.70
Structure
x-ray diffraction · 1 distinct chain · 19% helix, 32% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Histone-lysine N-methyltransferase 2D (EC 2.1.1.43) | protein | 161 | 19% helix, 32% strand | O14686 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 370 | 0.70 | 0.83 | 51 | SAH |
| 2 | 61 | 0.33 | 0.76 | 15 | empty |
Compared structures
- 4Z4P · Structure of the MLL4 SET Domain · 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 O14686
- Elsewhere: RCSB PDB 4Z4P · PDBe 4Z4P · UniProt O14686
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