Research workbench
Mycobacterium tuberculosis dihydrofolate reductase in complex with JEB285
Analyse Mycobacterium tuberculosis dihydrofolate reductase in complex with JEB285 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6VV8
- Type
- protein
- Length
- 318 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Dihydrofolate reductase
- EC
- 1.5.1.3
- UniProt
- A5U6B6
- Ligands
- NAP, RPV, CO
- Pockets
- 4 · best druggability 0.75
Structure
x-ray diffraction · 1 distinct chain · 19% helix, 35% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Dihydrofolate reductase (EC 1.5.1.3) | protein | 159 | 19% helix, 35% strand | A5U6B6 |
Ligands and binding sites
- NAP · Nadp nicotinamide-adenine-dinucleotide phosphate · ligand · 2 copies · chains A, B
- RPV · 5-{[3-(1H-indol-3-yl)propanoyl]amino}-1-phenyl-1H-pyrazole-4-carboxylic acid · ligand · 2 copies · chains A, B
- CO · Cobalt (II) ion · metal · 2 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, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 561 | 0.75 | 0.82 | 44 | NAP, RPV |
| 2 | 548 | 0.74 | 0.81 | 47 | NAP, RPV |
| 3 | 113 | 0.62 | 0.88 | 25 | empty |
| 4 | 137 | 0.61 | 0.85 | 27 | empty |
Interfaces
1 interface between chains.
- A–B · 980 Ų buried · 12 hydrogen bonds · protein-protein
Compared structures
- 6VV8 · Mycobacterium tuberculosis dihydrofolate reductase in complex with JEB285 · 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 A5U6B6
- Elsewhere: RCSB PDB 6VV8 · PDBe 6VV8 · UniProt A5U6B6
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.