1C09: Rubredoxin V44A cp

Rubredoxin V44A cp. Determined by X-ray diffraction at 1.6 Å resolution. Released 21 Feb 2001.

Method
X-ray diffraction
Resolution
1.6 Å
Organism
Clostridium pasteurianum
Chains
3
Atoms
1,391
Mol. weight
18.24 kDa
Ligands
FE
Released
21 Feb 2001

Explore 1C09 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1C09 contains 9 α-helices and 21 β-strands across 3 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.

Chains A, B and C: 3 helices, 7 β-strands

ElementResiduesLengthSheet
β-strand4-631
β-strand12-1321
β-strand1912
α-helix20-223
β-strand2412
α-helix30-323
β-strand3813
β-strand4513
α-helix46-483
β-strand49-5131

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
RubredoxinA, B, Cprotein54Clostridium pasteurianumP00268 (AlphaFold model)
Sequence of entity 1 (A, B, C), FASTA
>1C09_1 RUBREDOXIN (chains A, B, C)
MKKYTCTVCGYIYNPEDGDPDNGVNPGTDFKDIPDDWVCPLCGAGKDQFEEVEE

Ligands and cofactors

IDNameFormulaCopies
FEFE (III) ionFe3

Primary citation

Modulation of the redox potential of the [Fe(SCys)(4)] site in rubredoxin by the orientation of a peptide dipole. Eidsness, M.K., Burden, A.E., Richie, K.A. et al. Biochemistry (1999) 38:14803-14809. DOI 10.1021/bi991661f · PubMed

Other PDB entries of the same protein (UniProt P00268 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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