Research workbench
Ergothioneine-biosynthetic methyltransferase egtd in complex with pyrrolidinohistidine
Analyse Ergothioneine-biosynthetic methyltransferase egtd in complex with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6FNT
- 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
- AVO
- Pockets
- 3 · best druggability 0.77
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 | 42% 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
- AVO · Pyrrolidinohistidine · ligand · 2 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, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 960 | 0.77 | 0.79 | 75 | AVO |
| 2 | 990 | 0.75 | 0.78 | 82 | AVO |
| 3 | 212 | 0.57 | 0.80 | 37 | empty |
Interfaces
1 interface between chains.
- A–B · 721 Ų buried · 13 hydrogen bonds · protein-protein
Compared structures
- 6FNT · Ergothioneine-biosynthetic methyltransferase EgtD in complex with pyrrolidinohistidine · 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 6FNT · PDBe 6FNT · UniProt A0A0D6J225
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