› 1h8l

X-ray diffraction
2.6Å resolution

Duck Carboxypeptidase D Domain II in complex with GEMSA

Released:
DOI: 10.2210/pdb1h8l/pdb
PDB entry 1h8l coloured by chain, front view.
PDB entry 1h8l coloured by chain, side view.
PDB entry 1h8l coloured by chain, top view.
Source organism: Lophonetta specularioides
Primary publication:
The crystal structure of the inhibitor-complexed carboxypeptidase D domain II and the modeling of regulatory carboxypeptidases.
Aloy P, Companys V, Vendrell J, Aviles FX, Fricker LD, Coll M, Gomis-Rüth FX
J Biol Chem 276 16177-84 (2001)
PMID: 11278909

Function and Biology Details

Reaction catalysed: 
Releases C-terminal Arg and Lys from polypeptides.
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-160768 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (3 distinct):
Carboxypeptidase D Chain: A
Molecule details ›
Chain: A
Length: 380 amino acids
Theoretical weight: 43.34 KDa
Source organism: Lophonetta specularioides
Expression system: Komagataella pastoris
UniProt:
  • Canonical: P83852 (Residues: 1-380; Coverage: 100%)
Gene name: CPD
Sequence domains:
Structure domains:

Ligands and Environments

Carbohydrate polymer : NEW Components: NAG, BMA
Carbohydrate polymer
Carbohydrate polymer : NEW Components: NAG
Carbohydrate polymer
4 bound ligands:
Ligand GEM 1 x GEM
Ligand NAG 1 x NAG
Ligand SO4 1 x SO4
Ligand ZN 1 x ZN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE BW7B
Spacegroup: P213
Unit cell:
a: 136.48Å b: 136.48Å c: 136.48Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.199 0.199 0.239
Expression system: Komagataella pastoris

Quick links

Citations

7 review citations

Carboxypeptidase N: a pleiotropic regulator of inflammation.
Matthews et al. (2004)
6 more

7 mentions without citation

Evolutionary plasticity of protein families: coupling between sequence and structure variation.
Panchenko et al. (2005)
6 more