› 3knq

X-ray diffraction
2.13Å resolution

Beta Turn Optimization of the Gene-3-Protein of Filamentous Phage Fd

Released:
DOI: 10.2210/pdb3knq/pdb
PDB entry 3knq coloured by chain, front view.
PDB entry 3knq coloured by chain, side view.
PDB entry 3knq coloured by chain, top view.
Source organism: Enterobacteria phage fd
Primary publication:
Elimination of a cis-proline-containing loop and turn optimization stabilizes a protein and accelerates its folding.
Jakob RP, Zierer BK, Weininger U, Hofmann SD, Lorenz SH, Balbach J, Dobbek H, Schmid FX
J Mol Biol 399 331-46 (2010)
PMID: 20394751

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-137192 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Attachment protein G3P Chains: A, B
Molecule details ›
Chains: A, B
Length: 223 amino acids
Theoretical weight: 24.32 KDa
Source organism: Enterobacteria phage fd
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P03661 (Residues: 19-174, 181-238; Coverage: 53%)
Gene name: III
Sequence domains: Phage Coat Protein A
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BESSY BEAMLINE 14.1
Spacegroup: P212121
Unit cell:
a: 56.513Å b: 86.974Å c: 96.29Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.214 0.214 0.27
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

1 review citation

Principles and engineering of antibody folding and assembly.
Feige et al. (2014)
3 other articles

1 mention without citation

Cadmium-cysteine coordination in the BK inner pore region and its structural and functional implications.
Zhou et al. (2015)