MolNFT v1 · #24880 · protein
5,10-methylenetetrahydrofolate reductase from thermus thermophilus HB8
1V93: “5,10-methylenetetrahydrofolate reductase from thermus thermophilus HB8”. X-ray diffraction, 1 ligand (FAD), 2 pockets (best druggability 0.75). MolNFT v1 #24880 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1V93
- Type
- protein
- Length
- 292 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 5,10-methylenetetrahydrofolate reductase
- EC
- 1.7.99.5
- UniProt
- Q9RA47
- Ligands
- FAD
- Pockets
- 2 · best druggability 0.75
Structure
x-ray diffraction · 1 distinct chain · 48% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 5,10-methylenetetrahydrofolate reductase (EC 1.7.99.5) | protein | 292 | 48% helix, 14% strand | Q9RA47 |
Ligands and binding sites
- FAD · Flavin-adenine dinucleotide · ligand · chains A
- DIO · 1,4-diethylene dioxide · additive · 6 copies · chains A
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 | 734 | 0.75 | 0.80 | 56 | FAD |
| 2 | 74 | 0.41 | 0.79 | 17 | DIO |
Compared structures
- 1V93 · 5,10-Methylenetetrahydrofolate Reductase from Thermus thermophilus HB8 · 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 Q9RA47
- Elsewhere: RCSB PDB 1V93 · PDBe 1V93 · UniProt Q9RA47
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