› 1p4i

X-ray diffraction
2.8Å resolution

Crystal Structure of scFv against peptide GCN4

Released:
DOI: 10.2210/pdb1p4i/pdb
PDB entry 1p4i coloured by chain, front view.
PDB entry 1p4i coloured by chain, side view.
PDB entry 1p4i coloured by chain, top view.
Source organism: Mus musculus
Primary publication:
Directed in vitro evolution and crystallographic analysis of a peptide-binding single chain antibody fragment (scFv) with low picomolar affinity.
Zahnd C, Spinelli S, Luginbühl B, Amstutz P, Cambillau C, Plückthun A
J Biol Chem 279 18870-7 (2004)
PMID: 14754898

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-134499 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Ig lambda-1 chain V region Chain: L
Molecule details ›
Chain: L
Length: 135 amino acids
Theoretical weight: 13.33 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
UniProt:
  • Canonical: P01723 (Residues: 20-117; Coverage: 100%)
Sequence domains: Immunoglobulin V-set domain
Structure domains: Immunoglobulins
Ig heavy chain V region PJ14 Chain: H
Molecule details ›
Chain: H
Length: 124 amino acids
Theoretical weight: 13.45 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
UniProt:
  • Canonical: P01820 (Residues: 20-114; Coverage: 99%)
Sequence domains: Immunoglobulin V-set domain
Structure domains: Immunoglobulins

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P212121
Unit cell:
a: 35.089Å b: 60.533Å c: 123.055Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.2 0.2 0.26
Expression system: Escherichia coli

Quick links

Citations

26 review citations

Selecting and screening recombinant antibody libraries.
Hoogenboom HR. (2005)
25 more

5 mentions without citation

Electrostatic properties of protein-protein complexes.
Kundrotas et al. (2006)
4 more