1pp7

X-ray diffraction
2.45Å resolution

Crystal structure of the T. vaginalis Initiator binding protein bound to the ferredoxin Inr

Released:
Source organism: Trichomonas vaginalis

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
Entry contents:
1 distinct polypeptide molecule
2 distinct DNA molecules
Macromolecules (3 distinct):
39 kDa initiator binding protein Chain: U
Molecule details ›
Chain: U
Length: 131 amino acids
Theoretical weight: 15.21 KDa
Source organism: Trichomonas vaginalis
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q95VR4 (Residues: 1-126; Coverage: 37%)
Gene names: IBP39, TVAG_455080
Sequence domains: Transcription-initiator DNA-binding domain IBD
Structure domains: Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain
FERREDOXIN INR Chain: E
Molecule details ›
Chain: E
Length: 13 nucleotides
Theoretical weight: 3.93 KDa
Source organism: Trichomonas vaginalis
Expression system: Not provided
FERREDOXIN INR Chain: F
Molecule details ›
Chain: F
Length: 13 nucleotides
Theoretical weight: 4.01 KDa
Source organism: Trichomonas vaginalis
Expression system: Not provided

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL11-1
Spacegroup: P21212
Unit cell:
a: 81.34Å b: 41.43Å c: 58.39Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.197 0.197 0.246
Expression systems:
  • Escherichia coli BL21(DE3)
  • Not provided