D95A hydroquinone flavodoxin mutant from D. Vulgaris. Determined by X-ray diffraction at 1.9 Å resolution. Released 2 Dec 1998.
Explore 1AKU in 3D Show helices and sheets RCSB PDB PDBe
1AKU contains 8 α-helices and 8 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 | 3-9 | 7 | 1 |
| α-helix | 14-28 | 15 | |
| β-strand | 32-37 | 6 | 1 |
| α-helix | 38-40 | 3 | |
| β-strand | 52-57 | 6 | 1 |
| β-strand | 59-60 | 2 | 2 |
| β-strand | 66-67 | 2 | 2 |
| α-helix | 72-76 | 5 | |
| α-helix | 78-80 | 3 | |
| β-strand | 87-94 | 8 | 1 |
| α-helix | 103-114 | 12 | |
| β-strand | 118-119 | 2 | 1 |
| α-helix | 122-123 | 2 | |
| β-strand | 124-127 | 4 | 1 |
| α-helix | 130-132 | 3 | |
| α-helix | 134-147 | 14 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Flavodoxin | A | protein | 147 | Desulfovibrio vulgaris subsp. vulgaris str. Hildenborough | P00323 (AlphaFold model) |
>1AKU_1 FLAVODOXIN (chains A) PKALIVYGSTTGNTEYTAETIARELADAGYEVDSRDAASVEAGGLFEGFDLVLLGCSTWG DDSIELQDDFIPLFDSLEETGAQGRKVACFGCGASSYEYFCGAVDAIEEKLKNLGAEIVQ DGLRIDGDPRAARDDIVGWAHDVRGAI
| ID | Name | Formula | Copies |
|---|---|---|---|
| FMN | Flavin mononucleotide | C17 H21 N4 O9 P | 1 |
Water and common crystallization additives (SO4) are not listed.
Crystallographic investigation of the role of aspartate 95 in the modulation of the redox potentials of Desulfovibrio vulgaris flavodoxin. McCarthy, A.A., Walsh, M.A., Verma, C.S. et al. Biochemistry (2002) 41:10950-10962. DOI 10.1021/bi020225h · PubMed
Other PDB entries of the same protein (UniProt P00323 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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