MolNFT v1 · #167785 · protein
Mycobacterium tuberculosis dihydrofolate reductase in complex with JEB136
6VV7: “Mycobacterium tuberculosis dihydrofolate reductase in complex with JEB136”. X-ray diffraction, 5 ligands (NDP, RPM, CO). MolNFT v1 #167785 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6VV7
- Type
- protein
- Length
- 318 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- A5U6B6
- Ligands
- NDP, RPM, CO, PO4, SO4
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | — | protein | 159 | — | A5U6B6 |
Ligands and binding sites
- NDP · Nadph dihydro-nicotinamide-adenine-dinucleotide phosphate · ligand · 2 copies · chains A, B
- RPM · 5-[3-(5-methyl-1H-indol-3-yl)propoxy]-1-phenyl-1H-pyrazole-4-carboxylic acid · ligand · 2 copies · chains A, B
- CO · Cobalt (II) ion · metal · 2 copies · chains A, B
- PO4 · Phosphate ion · ion · 4 copies · chains A, B
- SO4 · Sulfate ion · ion · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6VV7 · Mycobacterium tuberculosis dihydrofolate reductase in complex with JEB136 · 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 6VV7 · PDBe 6VV7 · UniProt A5U6B6
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