› 1efp

X-ray diffraction
2.6Å resolution

ELECTRON TRANSFER FLAVOPROTEIN (ETF) FROM PARACOCCUS DENITRIFICANS

Released:
DOI: 10.2210/pdb1efp/pdb
PDB entry 1efp coloured by chain, front view.
PDB entry 1efp coloured by chain, side view.
PDB entry 1efp coloured by chain, top view.
Source organism: Paracoccus denitrificans
Primary publication:
Crystal structure of Paracoccus denitrificans electron transfer flavoprotein: structural and electrostatic analysis of a conserved flavin binding domain.
Roberts DL, Salazar D, Fulmer JP, Frerman FE, Kim JJ
Biochemistry 38 1977-89 (1999)
PMID: 10026281

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-153787 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Electron transfer flavoprotein subunit alpha Chains: A, C
Molecule details ›
Chains: A, C
Length: 307 amino acids
Theoretical weight: 31.19 KDa
Source organism: Paracoccus denitrificans
Expression system: Escherichia coli
UniProt:
  • Canonical: P38974 (Residues: 2-308; Coverage: 100%)
Gene name: etfA
Sequence domains:
Structure domains:
Electron transfer flavoprotein subunit beta Chains: B, D
Molecule details ›
Chains: B, D
Length: 252 amino acids
Theoretical weight: 26.71 KDa
Source organism: Paracoccus denitrificans
Expression system: Escherichia coli
UniProt:
  • Canonical: P38975 (Residues: 1-252; Coverage: 100%)
Gene name: etfB
Sequence domains: Electron transfer flavoprotein domain
Structure domains: HUPs

Ligands and Environments

2 bound ligands:
Ligand FAD 2 x FAD
Ligand AMP 2 x AMP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P212121
Unit cell:
a: 70.43Å b: 80.53Å c: 183.97Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.193 0.193 0.286
Expression system: Escherichia coli

Quick links

Citations

3 review citations

Sequence-structure analysis of FAD-containing proteins.
Dym et al. (2001)
2 more

10 mentions without citation

Chapter 4. Predicting and characterizing protein functions through matching geometric and evolutionary patterns of binding surfaces.
Liang et al. (2008)
9 more