3cfj

X-ray diffraction
2.6Å resolution

Crystal structure of catalytic elimination antibody 34E4, orthorhombic 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)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
CATALYTIC ANTIBODY FAB 34E4 LIGHT CHAIN fusion Chains: A, C, E, L
Molecule details ›
Chains: A, C, E, L
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
CATALYTIC ANTIBODY FAB 34E4 HEAVY CHAIN fusion Chains: B, D, F, H
Molecule details ›
Chains: B, D, F, H
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

2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.2.1
Spacegroup: P212121
Unit cell:
a: 81.137Å b: 114.471Å c: 212.131Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.202 0.199 0.253
Expression system: Escherichia coli