› 43ca

X-ray diffraction
2.3Å resolution

CRYSTALLOGRAPHIC STRUCTURE OF THE ESTEROLYTIC AND AMIDOLYTIC 43C9 ANTIBODY WITH BOUND P-NITROPHENOL

Released:
DOI: 10.2210/pdb43ca/pdb
PDB entry 43ca coloured by chain, front view.
PDB entry 43ca coloured by chain, side view.
PDB entry 43ca coloured by chain, top view.
Source organism: Mus musculus
Primary publication:
Structural basis for amide hydrolysis catalyzed by the 43C9 antibody.
Thayer MM, Olender EH, Arvai AS, Koike CK, Canestrelli IL, Stewart JD, Benkovic SJ, Getzoff ED, Roberts VA
J Mol Biol 291 329-45 (1999)
PMID: 10438624

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-208530 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
PROTEIN (IMMUNOGLOBULIN (LIGHT CHAIN)) Chains: A, C, E, G
Molecule details ›
Chains: A, C, E, G
Length: 113 amino acids
Theoretical weight: 12.43 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
Structure domains: Immunoglobulins
Ig heavy chain V region PJ14 Chains: B, D, F, H
Molecule details ›
Chains: B, D, F, H
Length: 117 amino acids
Theoretical weight: 12.79 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

1 bound ligand:
Ligand NPO 4 x NPO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL7-1
Spacegroup: C2221
Unit cell:
a: 106.25Å b: 110.86Å c: 244.42Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.206 0.206 0.259
Expression system: Escherichia coli

Quick links

Citations

5 review citations

Computational enzyme design.
Kiss et al. (2013)
4 more

5 mentions without citation

Protein surface charges and Ca2+ binding to individual sites in calbindin D9k: stopped-flow studies.
Martin et al. (1990)
4 more