1uwg

X-ray diffraction
2.79Å resolution

Molecular Mechanism of Enantioselective Proton Transfer to Carbon in Catalytic Antibody 14D9

Released:
Source organism: Mus musculus
Primary publication:
Molecular mechanism of enantioselective proton transfer to carbon in catalytic antibody 14D9.
Proc Natl Acad Sci U S A 101 3387-92 (2004)
PMID: 14988504

Function and Biology Details

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
PDBe Complex ID:
PDB-CPX-213099 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
ANTIBODY 14D9 Chains: H, Y
Molecule details ›
Chains: H, Y
Length: 225 amino acids
Theoretical weight: 23.93 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
Structure domains: Immunoglobulins
ANTIBODY 14D9 Chains: L, X
Molecule details ›
Chains: L, X
Length: 213 amino acids
Theoretical weight: 23.27 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
Structure domains: Immunoglobulins

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU300
Spacegroup: P21
Unit cell:
a: 68.47Å b: 97.92Å c: 70.88Å
α: 90° β: 99.28° γ: 90°
R-values:
R R work R free
0.207 0.204 0.276
Expression system: Escherichia coli