› 1dox

Solution NMR

1H AND 15N SEQUENTIAL ASSIGNMENT, SECONDARY STRUCTURE AND TERTIARY FOLD OF [2FE-2S] FERREDOXIN FROM SYNECHOCYSTIS SP. PCC 6803

Released:
DOI: 10.2210/pdb1dox/pdb
PDB entry 1dox coloured by chain, ensemble of 3 models, front view.
PDB entry 1dox coloured by chain, ensemble of 3 models, side view.
PDB entry 1dox coloured by chain, ensemble of 3 models, top view.
Source organism: Synechocystis sp. PCC 6803
Primary publication:
1H and 15N NMR sequential assignment, secondary structure, and tertiary fold of [2Fe-2S] ferredoxin from Synechocystis sp. PCC 6803.
Lelong C, Sétif P, Bottin H, André F, Neumann JM
Biochemistry 34 14462-73 (1995)
PMID: 7578051

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-150970 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ferredoxin-1 Chain: A
Molecule details ›
Chain: A
Length: 96 amino acids
Theoretical weight: 10.24 KDa
Source organism: Synechocystis sp. PCC 6803
UniProt:
  • Canonical: P27320 (Residues: 2-97; Coverage: 99%)
Gene names: fed, petF, ssl0020
Sequence domains: 2Fe-2S iron-sulfur cluster binding domain
Structure domains: Ubiquitin-like (UB roll)

Ligands and Environments

1 bound ligand:
Ligand FES 1 x FES
No modified residues

Experiments and Validation Details

Entry percentile scores

Quick links

Citations

3 review citations

The structure of iron-sulfur proteins.
Sticht et al. (1998)
2 more

1 mention without citation

The near-atomic cryoEM structure of a flexible filamentous plant virus shows homology of its coat protein with nucleoproteins of animal viruses.
Agirrezabala et al. (2015)