MolNFT v1 · #123482 · protein
Crystal structure of SETD2 bound to sah
5JLE · Histone-lysine N-methyltransferase SETD2: “Crystal structure of SETD2 bound to sah”. X-ray diffraction, 2 ligands (SAH, ZN), 2 pockets (best druggability 0.72). MolNFT v1 #123482 on GenesisL1: 3D structure, binding sites and pockets…
- PDB
- 5JLE
- Type
- protein
- Length
- 232 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Histone-lysine N-methyltransferase SETD2
- EC
- 2.1.1.43
- UniProt
- Q9BYW2
- Ligands
- SAH, ZN
- Pockets
- 2 · best druggability 0.72
Structure
x-ray diffraction · 1 distinct chain · 19% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Histone-lysine N-methyltransferase SETD2 (EC 2.1.1.43) | protein | 232 | 19% helix, 28% strand | Q9BYW2 |
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, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 336 | 0.72 | 0.84 | 43 | SAH |
| 2 | 106 | 0.56 | 0.84 | 17 | empty |
Compared structures
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 Q9BYW2
- Elsewhere: RCSB PDB 5JLE · PDBe 5JLE · UniProt Q9BYW2
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