Research workbench
Crystal structure of FAD-containing ferredoxin-NADP reductase from brucella ovis
Analyse Crystal structure of FAD-containing ferredoxin-NADP reductase from brucella ovis in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6RR3
- Type
- protein
- Length
- 257 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ferredoxin-NADP reductase
- EC
- 1.18.1.2
- UniProt
- A0A0H3ASL8
- Ligands
- FAD
- Pockets
- 2 · best druggability 0.66
Structure
x-ray diffraction · 1 distinct chain · 26% helix, 33% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ferredoxin-NADP reductase (EC 1.18.1.2) | protein | 257 | 26% helix, 33% strand | A0A0H3ASL8 |
Ligands and binding sites
- FAD · Flavin-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 | 371 | 0.66 | 0.80 | 44 | FAD |
| 2 | 87 | 0.35 | 0.75 | 20 | empty |
Compared structures
- 6RR3 · Crystal structure of FAD-containing ferredoxin-NADP reductase from brucella ovis · 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 A0A0H3ASL8
- Elsewhere: RCSB PDB 6RR3 · PDBe 6RR3 · UniProt A0A0H3ASL8
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