MolNFT v1 · #49104 · protein
P.AERUGINOSA fpr with FAD
2QDX · Ferredoxin reductase: “P.AERUGINOSA fpr with FAD”. X-ray diffraction, 2 ligands (FAD, SO4), 2 pockets (best druggability 0.66). MolNFT v1 #49104 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 2QDX
- Type
- protein
- Length
- 257 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ferredoxin reductase
- UniProt
- Q9HYK7
- Ligands
- FAD, SO4
- Pockets
- 2 · best druggability 0.66
Structure
x-ray diffraction · 1 distinct chain · 27% helix, 33% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ferredoxin reductase | protein | 257 | 27% helix, 33% strand | Q9HYK7 |
Ligands and binding sites
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 | 468 | 0.66 | 0.78 | 47 | SO4, FAD |
| 2 | 59 | 0.32 | 0.76 | 17 | empty |
Compared structures
- 2QDX · P.Aeruginosa Fpr with FAD · 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 Q9HYK7
- Elsewhere: RCSB PDB 2QDX · PDBe 2QDX · UniProt Q9HYK7
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