› 1aye

X-ray diffraction
1.8Å resolution

Function and Biology Details

Reaction catalysed: 
Similar to that of carboxypeptidase A (EC 3.4.17.1), but with a preference for bulkier C-terminal residues.
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-155697 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Carboxypeptidase A2 Chain: A
Molecule details ›
Chain: A
Length: 401 amino acids
Theoretical weight: 45.01 KDa
Source organism: Homo sapiens
Expression system: Komagataella pastoris
UniProt:
  • Canonical: P48052 (Residues: 19-419; Coverage: 100%)
Gene name: CPA2
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand ZN 1 x ZN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH2R
Spacegroup: P21
Unit cell:
a: 42.2Å b: 87.07Å c: 59.02Å
α: 90° β: 99.35° γ: 90°
R-values:
R R work R free
0.178 0.178 0.222
Expression system: Komagataella pastoris

Quick links

Citations

1 review citation

Structure and mechanism of metallocarboxypeptidases.
Gomis-Rüth FX. (2008)
43 other articles

21 mentions without citation

Practically useful: what the Rosetta protein modeling suite can do for you.
Kaufmann et al. (2010)
20 more