› 3dgs

X-ray diffraction
1.9Å resolution

Changing the determinants of protein stability from covalent to non-covalent interactions by in-vitro evolution: a structural and energetic analysis

Released:
DOI: 10.2210/pdb3dgs/pdb
PDB entry 3dgs coloured by chain, front view.
PDB entry 3dgs coloured by chain, side view.
PDB entry 3dgs coloured by chain, top view.
Source organism: Enterobacteria phage fd
Primary publication:
Changing the determinants of protein stability from covalent to non-covalent interactions by in vitro evolution: a structural and energetic analysis.
Kather I, Jakob R, Dobbek H, Schmid FX
J Mol Biol 381 1040-54 (2008)
PMID: 18621056

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: 227 amino acids
Theoretical weight: 24.78 KDa
Source organism: Enterobacteria phage fd
Expression system: Escherichia coli
UniProt:
  • Canonical: P03661 (Residues: 19-235; 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: BRUKER AXS MICROSTAR
Spacegroup: P212121
Unit cell:
a: 48.86Å b: 92.21Å c: 94.35Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.216 0.216 0.263
Expression system: Escherichia coli

Quick links

Citations

9 citation in other articles

Increased folding stability of TEM-1 beta-lactamase by in vitro selection.
Kather et al. (2008)
8 more

1 mention without citation

Engaging School and Family in Navajo Gardening for Health: Development of the Yéego Intervention to Promote Healthy Eating among Navajo Children.
Ornelas et al. (2021)