MolNFT v1 · #154915 · protein
NSD1 set domain in complex with SAM
6KQP · Histone-lysine N-methyltransferase, H3 lysine-36 and H4…: “NSD1 set domain in complex with SAM”. X-ray diffraction, 2 ligands (SAM, ZN), 3 pockets (best druggability 0.65). MolNFT v1 #154915 on GenesisL1: 3D structure, binding sites…
- PDB
- 6KQP
- Type
- protein
- Length
- 220 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Histone-lysine N-methyltransferase, H3 lysine-36 and H4 lysine-20 specific
- EC
- 2.1.1.357
- UniProt
- Q96L73
- Ligands
- SAM, ZN
- Pockets
- 3 · best druggability 0.65
Structure
x-ray diffraction · 1 distinct chain · 14% helix, 29% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Histone-lysine N-methyltransferase, H3 lysine-36 and H4 lysine-20 specific (EC 2.1.1.357) | protein | 220 | 14% helix, 29% strand | Q96L73 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 272 | 0.65 | 0.82 | 40 | SAM |
| 2 | 75 | 0.34 | 0.75 | 13 | empty |
| 3 | 51 | 0.30 | 0.76 | 13 | 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 Q96L73
- Elsewhere: RCSB PDB 6KQP · PDBe 6KQP · UniProt Q96L73
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