MolNFT v1 · #13881 · protein
Mycobacterium tuberculosis fpra in complex with NADPH
1LQU: “Mycobacterium tuberculosis fpra in complex with NADPH”. X-ray diffraction, 2 ligands (FAD, NDP), 6 pockets (best druggability 0.82). MolNFT v1 #13881 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1LQU
- Type
- protein
- Length
- 907 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Fpra
- UniProt
- O05783
- Ligands
- FAD, NDP
- Pockets
- 6 · best druggability 0.82
Structure
x-ray diffraction · 2 distinct chains · 38% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Fpra | protein | 453 | 38% helix, 21% strand | O05783 |
| B | Fpra | protein | 454 | 39% helix, 21% strand | O05783 |
Ligands and binding sites
- FAD · Flavin-adenine dinucleotide · ligand · 2 copies · chains A, B
- NDP · Nadph dihydro-nicotinamide-adenine-dinucleotide phosphate · ligand · 2 copies · chains A, B
- ACT · Acetate ion · additive · 11 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1057 | 0.82 | 0.83 | 122 | ACT, FAD, NDP |
| 2 | 1176 | 0.80 | 0.82 | 138 | ACT, FAD, NDP |
| 3 | 106 | 0.43 | 0.78 | 16 | empty |
| 4 | 53 | 0.42 | 0.82 | 13 | ACT |
| 5 | 92 | 0.40 | 0.77 | 18 | empty |
Interfaces
1 interface between chains.
- A–B · 1174 Ų buried · 16 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 covalent (additive adduct).
Compared structures
- 1LQU · Mycobacterium tuberculosis FprA in complex with NADPH · 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 O05783
- Elsewhere: RCSB PDB 1LQU · PDBe 1LQU · UniProt O05783
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