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Crystal structure of Ferredoxin reductase, BphA4 (oxidized form, NAD+ complex)
Analyse Crystal structure of Ferredoxin reductase, BphA4 (oxidized form, NAD+ complex) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2GR0
- Type
- protein
- Length
- 401 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.7
- Source
- Pseudomonas sp. KKS102
- Molecule
- ferredoxin reductase
- EC
- 1.18.1.2
- Ligands
- FAD, ADP
- Pockets
- 2 · best druggability 0.83
Structure
x-ray diffraction · resolution 1.7 · 1 distinct chain · 28% helix, 30% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | ferredoxin reductase (EC 1.18.1.2) | protein | 401 | 28% helix, 30% strand | — |
Ligands and binding sites
- FAD · Flavin-adenine dinucleotide · ligand · chains A
- ADP · Adenosine-5'-diphosphate · 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 | 659 | 0.83 | 0.87 | 86 | FAD, ADP |
| 2 | 120 | 0.48 | 0.79 | 17 | empty |
Compared structures
- 2GR0 · Crystal structure of ferredoxin reductase, BPHA4 (oxidized form, NAD+ complex) · 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
- Elsewhere: RCSB PDB 2GR0 · PDBe 2GR0
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