Research workbench
Methyltransferase bound with tetrahydrofolate
Analyse Methyltransferase bound with tetrahydrofolate in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2YCK
- Type
- protein
- Length
- 272 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 5-methyltetrahydrofolate CORRINOID/IRON sulfur protein methyltransferase
- UniProt
- Q3ACR9
- Ligands
- THG, SO4
- Pockets
- 2 · best druggability 0.58
Structure
x-ray diffraction · 1 distinct chain · 50% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| X | 5-methyltetrahydrofolate CORRINOID/IRON sulfur protein methyltransferase | protein | 272 | 50% helix, 14% strand | Q3ACR9 |
Ligands and binding sites
- THG · (6S)-5,6,7,8-tetrahydrofolate · ligand · chains X
- SO4 · Sulfate ion · ion · 7 copies · chains X
- GOL · Glycerol · additive · chains X
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 151 | 0.58 | 0.83 | 30 | empty |
| 2 | 289 | 0.54 | 0.76 | 39 | THG |
Compared structures
- 2YCK · methyltransferase bound with tetrahydrofolate · the same entry in another collection · chain X against X, 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 Q3ACR9
- Elsewhere: RCSB PDB 2YCK · PDBe 2YCK · UniProt Q3ACR9
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