Research workbench
Pea fnr Y308W mutant in complex with NADP+
Analyse Pea fnr Y308W mutant in complex with NADP+ in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1QGA
- Type
- protein
- Length
- 603 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein (FERREDOXIN:NADP+ reductase)
- EC
- 1.18.1.2
- UniProt
- P10933
- Ligands
- FAD, NAP, SO4
- Pockets
- 6 · best druggability 0.62
Structure
x-ray diffraction · 2 distinct chains · 26% helix, 31% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein (FERREDOXIN:NADP+ reductase) (EC 1.18.1.2) | protein | 308 | 25% helix, 30% strand | P10933 |
| B | Protein (FERREDOXIN:NADP+ reductase) (EC 1.18.1.2) | protein | 295 | 26% helix, 32% strand | P10933 |
Ligands and binding sites
- FAD · Flavin-adenine dinucleotide · ligand · 2 copies · chains A, B
- NAP · Nadp nicotinamide-adenine-dinucleotide phosphate · ligand · 2 copies · chains A, B
- SO4 · Sulfate ion · ion · 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, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 588 | 0.62 | 0.73 | 53 | empty |
| 2 | 281 | 0.57 | 0.77 | 44 | FAD, NAP |
| 3 | 176 | 0.51 | 0.78 | 29 | NAP |
| 4 | 89 | 0.36 | 0.75 | 18 | FAD |
| 5 | 53 | 0.34 | 0.78 | 21 | empty |
Interfaces
1 interface between chains.
- A–B · 399 Ų buried · 3 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 covalent (covalent ligand).
Compared structures
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 P10933
- Elsewhere: RCSB PDB 1QGA · PDBe 1QGA · UniProt P10933
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