Research workbench
Crystal structure of ferredoxin reductase, BPHA4 (blue-semiquinone)
Analyse Crystal structure of ferredoxin reductase, BPHA4 (blue-semiquinone) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2YVG
- Type
- protein
- Length
- 401 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ferredoxin reductase
- EC
- 1.18.1.2
- UniProt
- Q52437
- Ligands
- FAD, NAD
- Pockets
- 2 · best druggability 0.83
Structure
x-ray diffraction · 1 distinct chain · 27% helix, 29% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ferredoxin reductase (EC 1.18.1.2) | protein | 401 | 27% helix, 29% strand | Q52437 |
Ligands and binding sites
- FAD · Flavin-adenine dinucleotide · ligand · chains A
- NAD · Nicotinamide-adenine-dinucleotide · ligand · 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 | 742 | 0.83 | 0.86 | 86 | FAD, NAD |
| 2 | 115 | 0.49 | 0.80 | 17 | empty |
Compared structures
- 2YVG · crystal structure of ferredoxin reductase, BPHA4 (blue-semiqui ) · 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 Q52437
- Elsewhere: RCSB PDB 2YVG · PDBe 2YVG · UniProt Q52437
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