MolNFT v1 · #149020 · protein
Ergothioneine-biosynthetic methyltransferase egtd in complex with N,N, N-trimethylhistidine (hercynine)
6FNQ · Histidine N-alpha-methyltransferase: “Ergothioneine-biosynthetic methyltransferase egtd in complex with N,N, N-trimethylhistidine (hercynine)”. X-ray diffraction, 2 ligands (AVJ, MG), 4 pockets (best druggability 0.76). MolNFT v1…
- PDB
- 6FNQ
- Type
- protein
- Length
- 645 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Histidine N-alpha-methyltransferase
- EC
- 2.1.1.44
- UniProt
- A0A0D6J225
- Ligands
- AVJ, MG
- Pockets
- 4 · best druggability 0.76
Structure
x-ray diffraction · 2 distinct chains · 43% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Histidine N-alpha-methyltransferase (EC 2.1.1.44) | protein | 322 | 43% helix, 27% strand | A0A0D6J225 |
| B | Histidine N-alpha-methyltransferase (EC 2.1.1.44) | protein | 323 | 43% helix, 27% strand | A0A0D6J225 |
Ligands and binding sites
- AVJ · N,N,N-trimethyl-histidine · ligand · 2 copies · chains A, B
- MG · Magnesium ion · metal · chains A
- GOL · Glycerol · additive · 6 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 | 895 | 0.76 | 0.79 | 71 | AVJ, GOL |
| 2 | 998 | 0.75 | 0.78 | 81 | AVJ, GOL |
| 3 | 92 | 0.46 | 0.81 | 20 | GOL |
| 4 | 100 | 0.45 | 0.80 | 18 | GOL |
Interfaces
1 interface between chains.
- A–B · 716 Ų buried · 12 hydrogen bonds · protein-protein
Compared structures
- 6FNQ · Ergothioneine-biosynthetic methyltransferase EgtD in complex with… · 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 A0A0D6J225
- Elsewhere: RCSB PDB 6FNQ · PDBe 6FNQ · UniProt A0A0D6J225
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