5aq0

X-ray diffraction
0.95Å resolution

The structure of the Transthyretin-like domain of the first catalytic domain of the HUMAN Carboxypeptidase D

Released:
Source organism: Homo sapiens
Entry authors: Gallego P, Garcia-Pardo J, Lorenzo J, Aviles FX, Ventura S, Reverter D

Function and Biology Details

Reaction catalysed:
Releases C-terminal Arg and Lys from polypeptides.
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Carboxypeptidase D Chains: A, B
Molecule details ›
Chains: A, B
Length: 82 amino acids
Theoretical weight: 8.76 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: O75976 (Residues: 383-461; Coverage: 6%)
Gene name: CPD
Structure domains: Carboxypeptidase-like, regulatory domain

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALBA BEAMLINE XALOC
Spacegroup: P21
Unit cell:
a: 39.773Å b: 46.051Å c: 42.73Å
α: 90° β: 90.18° γ: 90°
R-values:
R R work R free
0.154 0.153 0.175
Expression system: Escherichia coli BL21