1AKR: G61A oxidized flavodoxin mutant

G61A oxidized flavodoxin mutant. Determined by X-ray diffraction at 1.58 Å resolution. Released 27 May 1998.

Method
X-ray diffraction
Resolution
1.58 Å
Organism
Desulfovibrio vulgaris subsp. vulgaris str. Hildenborough
Chains
1
Atoms
1,246
Mol. weight
16.17 kDa
Ligands
FMN
Released
27 May 1998

Explore 1AKR in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1AKR 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.

Chain A: 8 helices, 8 β-strands

ElementResiduesLengthSheet
β-strand3-971
α-helix14-2714
β-strand32-3761
α-helix38-403
β-strand52-5761
β-strand5912
β-strand6712
α-helix72-765
α-helix78-803
β-strand87-9481
α-helix103-11412
β-strand118-11921
α-helix122-1232
β-strand124-12741
α-helix130-1334
α-helix134-14714

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
FlavodoxinAprotein147Desulfovibrio vulgaris subsp. vulgaris str. HildenboroughP00323 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>1AKR_1 FLAVODOXIN (chains A)
PKALIVYGSTTGNTEYTAETIARELADAGYEVDSRDAASVEAGGLFEGFDLVLLGCSTWA
DDSIELQDDFIPLFDSLEETGAQGRKVACFGCGDSSYEYFCGAVDAIEEKLKNLGAEIVQ
DGLRIDGDPRAARDDIVGWAHDVRGAI

Ligands and cofactors

IDNameFormulaCopies
FMNFlavin mononucleotideC17 H21 N4 O9 P1

Primary citation

Modulation of the redox potentials of FMN in Desulfovibrio vulgaris flavodoxin: thermodynamic properties and crystal structures of glycine-61 mutants. O'Farrell, P.A., Walsh, M.A., McCarthy, A.A. et al. Biochemistry (1998) 37:8405-8416. DOI 10.1021/bi973193k · 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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