Ferredoxin:nadp+ oxidoreductase (ferredoxin reductase) mutant E312A. Determined by X-ray diffraction at 1.95 Å resolution. Released 14 Oct 1998.
Explore 1FRQ in 3D Show helices and sheets RCSB PDB PDBe
1FRQ contains 13 α-helices and 24 β-strands across 1 chain. 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 |
|---|---|---|---|
| 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 |
| β-strand | 89 | 1 | 5 |
| α-helix | 90-92 | 3 | |
| β-strand | 93-96 | 4 | 4 |
| β-strand | 110-116 | 7 | 4 |
| α-helix | 117-118 | 2 | |
| β-strand | 119-121 | 3 | 6 |
| β-strand | 127-129 | 3 | 6 |
| α-helix | 131-138 | 8 | |
| 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 | 189 | 1 | 8 |
| β-strand | 192 | 1 | 8 |
| 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 | 9 |
| β-strand | 244 | 1 | 9 |
| α-helix | 247-252 | 6 | |
| α-helix | 255-262 | 8 | |
| β-strand | 267-273 | 7 | 7 |
| α-helix | 276-290 | 15 | |
| α-helix | 296-305 | 10 | |
| β-strand | 309-313 | 5 | 7 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Protein (ferredoxin:nadp+ oxidoreductase) | A | protein | 314 | Spinacia oleracea | P00455 (AlphaFold model) |
>1FRQ_1 PROTEIN (FERREDOXIN:NADP+ OXIDOREDUCTASE) (chains A) QIASDVEAPPPAPAKVEKHSKKMEEGITVNKFKPKTPYVGRCLLNTKITGDDAPGETWHM VFSHEGEIPYREGQSVGVIPDGEDKNGKPHKLRLYSIASSALGDFGDAKSVSLCVKRLIY TNDAGETIKGVCSNFLCDLKPGAEVKLTGPVGKEMLMPKDPNATIIMLGTGTGIAPFRSF LWKMFFEKHDDYKFNGLAWLFLGVPTSSSLLYKEEFEKMKEKAPDNFRLDFAVSREQTNE KGEKMYIQTRMAQYAVELWEMLKKDNTYFYMCGLKGMEKGIDDIMVSLAAAEGIDWIEYK RQLKKAEQWNVAVY
Water and common crystallization additives (SO4) are not listed.
Probing the function of the invariant glutamyl residue 312 in spinach ferredoxin-NADP+ reductase. Aliverti, A., Deng, Z., Ravasi, D. et al. J Biol Chem (1998) 273:34008-34015. DOI 10.1074/jbc.273.51.34008 · PubMed
Other PDB entries of the same protein (UniProt P00455 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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