Rubredoxin V44A cp. Determined by X-ray diffraction at 1.6 Å resolution. Released 21 Feb 2001.
Explore 1C09 in 3D Show helices and sheets RCSB PDB PDBe
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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 4-6 | 3 | 1 |
| β-strand | 12-13 | 2 | 1 |
| β-strand | 19 | 1 | 2 |
| α-helix | 20-22 | 3 | |
| β-strand | 24 | 1 | 2 |
| α-helix | 30-32 | 3 | |
| β-strand | 38 | 1 | 3 |
| β-strand | 45 | 1 | 3 |
| α-helix | 46-48 | 3 | |
| β-strand | 49-51 | 3 | 1 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Rubredoxin | A, B, C | protein | 54 | Clostridium pasteurianum | P00268 (AlphaFold model) |
>1C09_1 RUBREDOXIN (chains A, B, C) MKKYTCTVCGYIYNPEDGDPDNGVNPGTDFKDIPDDWVCPLCGAGKDQFEEVEE
| ID | Name | Formula | Copies |
|---|---|---|---|
| FE | FE (III) ion | Fe | 3 |
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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