MolNFT v1 · #58621 · protein
EUHMT1 (glp) ankyrin repeat domain (structure 2)
3B95 · Euchromatic histone-lysine N-methyltransferase 1: “EUHMT1 (glp) ankyrin repeat domain (structure 2)”. X-ray diffraction, 1 ligand (SO4), 3 pockets (best druggability 0.64). MolNFT v1 #58621 on GenesisL1: 3D structure, binding sites…
- PDB
- 3B95
- Type
- protein
- Length
- 471 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Euchromatic histone-lysine N-methyltransferase 1; Histone H3 N-terminal peptide
- UniProt
- Q5VT56
- Ligands
- SO4
- Pockets
- 3 · best druggability 0.64
Structure
x-ray diffraction · 3 distinct chains · 47% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Euchromatic histone-lysine N-methyltransferase 1 | protein | 236 | 47% helix, 1% strand | Q5VT56 |
| B | Euchromatic histone-lysine N-methyltransferase 1 | protein | 225 | 49% helix, 0% strand | Q5VT56 |
| P | Histone H3 N-terminal peptide | protein | 10 | 0% helix, 0% strand | — |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 10 copies · chains A, B
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 | 442 | 0.64 | 0.77 | 39 | empty |
| 2 | 71 | 0.37 | 0.78 | 18 | empty |
| 3 | 58 | 0.32 | 0.76 | 17 | empty |
Interfaces
2 interfaces between chains.
- B–P · 640 Ų buried · 11 hydrogen bonds · protein-protein
- A–B · 172 Ų buried · 3 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 modified (methylation).
Compared structures
- 3B95 · EuHMT1 (Glp) Ankyrin Repeat Domain (Structure 2) · the same entry in another collection · chain A against A, TM-score 1.00
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 Q5VT56
- Elsewhere: RCSB PDB 3B95 · PDBe 3B95 · UniProt Q5VT56
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