2pvg

X-ray diffraction
2.4Å resolution

Crystal srtucture of the binary complex between ferredoxin and ferredoxin:thioredoxin reductase

Released:

Function and Biology Details

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
PDBe Complex ID:
PDB-CPX-150971 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Ferredoxin-thioredoxin reductase, catalytic chain Chain: A
Molecule details ›
Chain: A
Length: 108 amino acids
Theoretical weight: 12.27 KDa
Source organism: Synechocystis sp.
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q55389 (Residues: 11-116; Coverage: 90%)
Gene names: ftrC, sll0554
Sequence domains: Ferredoxin thioredoxin reductase catalytic beta chain
Structure domains: Ferredoxin thioredoxin reductase catalytic beta subunit
Ferredoxin-thioredoxin reductase, variable chain Chain: B
Molecule details ›
Chain: B
Length: 73 amino acids
Theoretical weight: 8.11 KDa
Source organism: Synechocystis sp.
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q55781 (Residues: 1-73; Coverage: 97%)
Gene names: ftrV, ssr0330
Sequence domains: Ferredoxin thioredoxin reductase variable alpha chain
Structure domains: SH3 type barrels.
Ferredoxin-1 Chain: C
Molecule details ›
Chain: C
Length: 96 amino acids
Theoretical weight: 10.25 KDa
Source organism: Synechocystis sp.
Expression system: Escherichia coli BL21
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

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: C2221
Unit cell:
a: 63.462Å b: 89.702Å c: 99.303Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.238 0.238 0.288
Expression system: Escherichia coli BL21