Crystal structure analysis of the ferredoxin-NADP+ reductase from maize leaf. Determined by X-ray diffraction at 2.2 Å resolution. Released 7 Feb 2001.
Explore 1GAW in 3D Show helices and sheets RCSB PDB PDBe
1GAW contains 30 α-helices and 44 β-strands across 2 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 18-20 | 3 | |
| β-strand | 22 | 1 | 1 |
| β-strand | 32 | 1 | 2 |
| β-strand | 33 | 1 | 3 |
| β-strand | 36 | 1 | 3 |
| β-strand | 38-47 | 10 | 4 |
| β-strand | 57-63 | 7 | 4 |
| β-strand | 75-79 | 5 | 4 |
| β-strand | 83 | 1 | 5 |
| α-helix | 88 | 1 | |
| β-strand | 89 | 1 | 5 |
| α-helix | 90-92 | 3 | |
| β-strand | 93-97 | 5 | 4 |
| β-strand | 110-116 | 7 | 4 |
| β-strand | 119-121 | 3 | 6 |
| β-strand | 127-129 | 3 | 6 |
| α-helix | 131-137 | 7 | |
| β-strand | 144-151 | 8 | 4 |
| α-helix | 156-157 | 2 | |
| β-strand | 158 | 1 | 1 |
| β-strand | 164-170 | 7 | 7 |
| α-helix | 171-174 | 4 | |
| α-helix | 175-181 | 7 | |
| α-helix | 182-186 | 5 | |
| β-strand | 197-204 | 8 | 7 |
| α-helix | 207-209 | 3 | |
| α-helix | 213-222 | 10 | |
| β-strand | 227-233 | 7 | 7 |
| β-strand | 238 | 1 | 8 |
| β-strand | 244 | 1 | 8 |
| α-helix | 247-251 | 5 | |
| α-helix | 252-254 | 3 | |
| α-helix | 255-262 | 8 | |
| β-strand | 267-273 | 7 | 7 |
| α-helix | 277-289 | 13 | |
| α-helix | 296-305 | 10 | |
| β-strand | 309-313 | 5 | 7 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 22 | 1 | 9 |
| β-strand | 32 | 1 | 10 |
| β-strand | 33 | 1 | 11 |
| β-strand | 36 | 1 | 11 |
| β-strand | 38-47 | 10 | 12 |
| β-strand | 57-63 | 7 | 12 |
| β-strand | 75-79 | 5 | 12 |
| β-strand | 83 | 1 | 13 |
| α-helix | 88 | 1 | |
| β-strand | 89 | 1 | 13 |
| α-helix | 90-92 | 3 | |
| β-strand | 93-97 | 5 | 12 |
| β-strand | 110-116 | 7 | 12 |
| β-strand | 119-121 | 3 | 14 |
| β-strand | 127-129 | 3 | 14 |
| α-helix | 131-137 | 7 | |
| β-strand | 144-151 | 8 | 12 |
| α-helix | 156-157 | 2 | |
| β-strand | 158 | 1 | 9 |
| β-strand | 164-170 | 7 | 15 |
| α-helix | 171-174 | 4 | |
| α-helix | 175-181 | 7 | |
| α-helix | 182-186 | 5 | |
| β-strand | 197-204 | 8 | 15 |
| α-helix | 207-209 | 3 | |
| α-helix | 213-222 | 10 | |
| β-strand | 227-233 | 7 | 15 |
| β-strand | 238 | 1 | 16 |
| β-strand | 244 | 1 | 16 |
| α-helix | 247-251 | 5 | |
| α-helix | 252-254 | 3 | |
| α-helix | 257-262 | 6 | |
| β-strand | 267-273 | 7 | 15 |
| α-helix | 277-289 | 13 | |
| α-helix | 290-292 | 3 | |
| α-helix | 296-305 | 10 | |
| β-strand | 309-313 | 5 | 15 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Ferredoxin-NADP+ reductase | A, B | protein | 314 | Zea mays | Q9SLP6 (AlphaFold model) |
>1GAW_1 FERREDOXIN-NADP+ REDUCTASE (chains A, B) IRAQASAVEAPATAKAKKESKKQEEGVVTNLYKPKEPYVGRCLLNTKITGDDAPGETWHM VFSTEGKIPYREGQSIGVIADGVDKNGKPHKVRLYSIASSAIGDFGDSKTVSLCVKRLIY TNDAGEIVKGVCSNFLCDLQPGDNVQITGPVGKEMLMPKDPNATIIMLATGTGIAPFRSF LWKMFFEKHDDYKFNGLGWLFLGVPTSSSLLYKEEFGKMKERAPENFRVDYAVSREQTNA AGERMYIQTRMAEYKEELWELLKKDNTYVYMCGLKGMEKGIDDIMVSLAEKDGIDWFDYK KQLKRGDQWNVEVY
| ID | Name | Formula | Copies |
|---|---|---|---|
| FAD | Flavin-adenine dinucleotide | C27 H33 N9 O15 P2 | 2 |
Structure of the electron transfer complex between ferredoxin and ferredoxin-NADP(+) reductase. Kurisu, G., Kusunoki, M., Katoh, E. et al. Nat Struct Biol (2001) 8:117-121. DOI 10.1038/84097 · PubMed
Other PDB entries of the same protein (UniProt Q9SLP6 (AlphaFold model), which also has an AlphaFold model), best resolution first:
MolViewer shows 1GAW directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.