Research workbench
Crystal structure of EHMT2 set domain in complex with compound 5.
Analyse Crystal structure of EHMT2 set domain in complex with compound 5. in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7BTV
- Type
- protein
- Length
- 545 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q96KQ7
- Ligands
- N47, ZN
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 272 | — | Q96KQ7 |
| B | — | protein | 273 | — | Q96KQ7 |
Ligands and binding sites
- N47 · N~2~-{4-methoxy-3-[3-(pyrrolidin-1-yl)propoxy]phenyl}-N~4~,6-dimethylpyrimidine-2,4-diamine · ligand · 2 copies · chains A, B
- ZN · Zinc ion · metal · 8 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 7BTV · Crystal structure of EHMT2 SET domain in complex with compound 5. · the same entry in another collection · chain B against B, TM-score 1.00
- Q96KQ7 · AlphaFold monomer V2.0 prediction for histone-lysine N-methyltransferase EHMT2 (Q96KQ7) · a predicted model of the same protein · chain A against A, TM-score 0.99
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 Q96KQ7
- Elsewhere: RCSB PDB 7BTV · PDBe 7BTV · UniProt Q96KQ7
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