› 2boa

X-ray diffraction
2.2Å resolution

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-193778 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Carboxypeptidase A4 Chains: A, B
Molecule details ›
Chains: A, B
Length: 404 amino acids
Theoretical weight: 45.61 KDa
Source organism: Homo sapiens
Expression system: Komagataella pastoris
UniProt:
  • Canonical: Q9UI42 (Residues: 18-421; Coverage: 100%)
Gene names: CPA3, CPA4, UNQ694/PRO1339
Sequence domains:
Structure domains:

Ligands and Environments

Carbohydrate polymer : NEW Components: NAG
Carbohydrate polymer
3 bound ligands:
Ligand NAG 1 x NAG
Ligand ZN 2 x ZN
Ligand GOL 4 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID29
Spacegroup: C2
Unit cell:
a: 136.8Å b: 87.2Å c: 89.7Å
α: 90° β: 117.2° γ: 90°
R-values:
R R work R free
0.221 0.22 0.293
Expression system: Komagataella pastoris

Quick links

Citations

4 review citations

Structure and mechanism of metallocarboxypeptidases.
Gomis-Rüth FX. (2008)
3 more

4 mentions without citation

Effects of Glycosylation on the Enzymatic Activity and Mechanisms of Proteases.
Goettig P. (2016)
3 more