MolNFT v1 · #174915 · protein
Crystal structure of SETDB1 tudor domain in complexed with compound 2.
7CAJ · Histone-lysine N-methyltransferase SETDB1: “Crystal structure of SETDB1 tudor domain in complexed with compound 2.”. X-ray diffraction, 1 ligand (FNC), 5 pockets (best druggability 0.85). MolNFT v1 #174915 on GenesisL1: 3D…
- PDB
- 7CAJ
- Type
- protein
- Length
- 422 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Histone-lysine N-methyltransferase SETDB1
- EC
- 2.1.1.-
- UniProt
- Q15047
- Ligands
- FNC
- Pockets
- 5 · best druggability 0.85
Structure
x-ray diffraction · 1 distinct chain · 14% helix, 46% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| D, A | Histone-lysine N-methyltransferase SETDB1 (EC 2.1.1.-) | protein | 211 | 14% helix, 46% strand | Q15047 |
Ligands and binding sites
- FNC · 3-methyl-2-[[(3R,5R)-1-methyl-5-phenyl-piperidin-3-yl]amino]-5H-pyrrolo[3,2-d]pyrimidin-4-one · ligand · 2 copies · chains D, A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1142 | 0.85 | 0.86 | 87 | FNC |
| 2 | 51 | 0.33 | 0.78 | 15 | empty |
| 3 | 51 | 0.32 | 0.77 | 15 | empty |
| 4 | 67 | 0.31 | 0.75 | 17 | empty |
| 5 | 53 | 0.26 | 0.73 | 15 | empty |
Interfaces
1 interface between chains.
- D–A · 865 Ų buried · 5 hydrogen bonds · protein-protein
Compared structures
- 7CAJ · Crystal structure of SETDB1 Tudor domain in complexed with Compound 2. · the same entry in another collection · chain D against D, TM-score 1.00
- Q15047 · AlphaFold monomer V2.0 prediction for histone-lysine N-methyltransferase SETDB1 (Q15047) · a predicted model of the same protein · chain D against A, TM-score 0.98
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 Q15047
- Elsewhere: RCSB PDB 7CAJ · PDBe 7CAJ · UniProt Q15047
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