MolNFT v1 · #58556 · protein
EUHMT1 (glp) ankyrin repeat domain (structure 1)
3B7B · Euchromatic histone-lysine N-methyltransferase 1: “EUHMT1 (glp) ankyrin repeat domain (structure 1)”. X-ray diffraction, 1 ligand (SO4), 2 pockets (best druggability 0.62). MolNFT v1 #58556 on GenesisL1: 3D structure, binding sites…
- PDB
- 3B7B
- Type
- protein
- Length
- 460 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Euchromatic histone-lysine N-methyltransferase 1
- EC
- 2.1.1.43
- UniProt
- Q9H9B1
- Ligands
- SO4
- Pockets
- 2 · best druggability 0.62
Structure
x-ray diffraction · 2 distinct chains · 49% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Euchromatic histone-lysine N-methyltransferase 1 (EC 2.1.1.43) | protein | 236 | 47% helix, 0% strand | Q9H9B1 |
| B | Euchromatic histone-lysine N-methyltransferase 1 (EC 2.1.1.43) | protein | 224 | 50% helix, 0% strand | Q9H9B1 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 8 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 412 | 0.62 | 0.77 | 38 | empty |
| 2 | 56 | 0.36 | 0.79 | 18 | empty |
Interfaces
1 interface between chains.
- A–B · 164 Ų buried · 1 hydrogen bond · protein-protein
Compared structures
- 3B7B · EuHMT1 (Glp) Ankyrin Repeat Domain (Structure 1) · the same entry in another collection · chain A against A, TM-score 1.00
- Q9H9B1 · AlphaFold monomer V2.0 prediction for histone-lysine N-methyltransferase EHMT1 (Q9H9B1) · a predicted model of the same protein · chain B 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 Q9H9B1
- Elsewhere: RCSB PDB 3B7B · PDBe 3B7B · UniProt Q9H9B1
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