3cfk

X-ray diffraction
2.6Å resolution

Crystal structure of catalytic elimination antibody 34E4, triclinic crystal form

Released:
Source organism: Mus musculus
Primary publication:
Conformational isomerism can limit antibody catalysis.
J Biol Chem 283 16554-60 (2008)
PMID: 18417480

Function and Biology Details

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
PDBe Complex ID:
PDB-CPX-179926 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Ig-like domain-containing protein Chains: A, C, E, G, J, L, M, O
Molecule details ›
Chains: A, C, E, G, J, L, M, O
Length: 216 amino acids
Theoretical weight: 23.26 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
UniProt:
  • Canonical: Q8TCD0 (Residues: 21-239; Coverage: 99%)
Sequence domains:
Structure domains: Immunoglobulins
Ig-like domain-containing protein Chains: B, D, F, H, I, K, N, P
Molecule details ›
Chains: B, D, F, H, I, K, N, P
Length: 227 amino acids
Theoretical weight: 24.7 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
UniProt:
  • Canonical: Q6N089 (Residues: 20-117, 118-246; Coverage: 50%)
Gene name: DKFZp686P15220
Sequence domains:
Structure domains: Immunoglobulins

Ligands and Environments

3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL9-2
Spacegroup: P1
Unit cell:
a: 81.069Å b: 106.299Å c: 116.109Å
α: 89.89° β: 90.04° γ: 89.48°
R-values:
R R work R free
0.222 0.221 0.244
Expression system: Escherichia coli