MolNFT v1 · #116955 · protein
Crystal structure of DOT1L in complex with inhibitor CPD5 [N-(2,6- dichlorophenyl)-4-methoxy-N-methylquinolin-6-amine]
5DTR · Histone-lysine N-methyltransferase, H3 lysine-79 specific: “Crystal structure of DOT1L in complex with inhibitor CPD5 [N-(2,6…”. X-ray diffraction, 1 ligand (5F7), 4 pockets (best druggability 0.89). MolNFT v1 #116955 on GenesisL1…
- PDB
- 5DTR
- Type
- protein
- Length
- 638 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Histone-lysine N-methyltransferase, H3 lysine-79 specific
- EC
- 2.1.1.43
- UniProt
- Q8TEK3
- Ligands
- 5F7
- Pockets
- 4 · best druggability 0.89
Structure
x-ray diffraction · 2 distinct chains · 45% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Histone-lysine N-methyltransferase, H3 lysine-79 specific (EC 2.1.1.43) | protein | 319 | 44% helix, 15% strand | Q8TEK3 |
| B | Histone-lysine N-methyltransferase, H3 lysine-79 specific (EC 2.1.1.43) | protein | 319 | 45% helix, 15% strand | Q8TEK3 |
Ligands and binding sites
- 5F7 · N-(2,6-dichlorophenyl)-4-methoxy-N-methylquinolin-6-amine · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1092 | 0.89 | 0.90 | 130 | 5F7 |
| 2 | 248 | 0.60 | 0.80 | 34 | empty |
| 3 | 92 | 0.49 | 0.82 | 17 | empty |
| 4 | 84 | 0.34 | 0.75 | 16 | empty |
Interfaces
1 interface between chains.
- A–B · 1506 Ų buried · 17 hydrogen bonds · protein-protein
Compared structures
- 5DTR · Crystal structure of Dot1L in complex with inhibitor CPD5… · the same entry in another collection · chain A against A, TM-score 1.00
- Q8TEK3 · AlphaFold monomer V2.0 prediction for histone-lysine N-methyltransferase, H3 lysine-79… · a predicted model of the same protein · chain B against A, TM-score 0.94
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 Q8TEK3
- Elsewhere: RCSB PDB 5DTR · PDBe 5DTR · UniProt Q8TEK3
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