› 6i6z

X-ray diffraction
1.72Å resolution

Crystal structure of the human CARBOXYPEPTIDASE A1 in complex with the PHOSPHINIC INHIBITOR Acetyl-Tyr-Ala-Y(PO2CH2)-homoPhe-OH

Released:
DOI: 10.2210/pdb6i6z/pdb
PDB entry 6i6z coloured by chain, front view.
PDB entry 6i6z coloured by chain, side view.
PDB entry 6i6z coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Synthesis and Structural/Functional Characterization of Selective M14 Metallocarboxypeptidase Inhibitors Based on Phosphinic Pseudopeptide Scaffold: Implications on the Design of Specific Optical Probes.
Covaleda G, Gallego P, Vendrell J, Georgiadis D, Lorenzo J, Dive V, Aviles FX, Reverter D, Devel L
J Med Chem 62 1917-1931 (2019)
PMID: 30688452

Function and Biology Details

Reaction catalysed: 
Release of a C-terminal amino acid, but little or no action with -Asp, -Glu, -Arg, -Lys or -Pro.
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-147210 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Carboxypeptidase A1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 308 amino acids
Theoretical weight: 34.54 KDa
Source organism: Homo sapiens
Expression system: Komagataella pastoris
UniProt:
  • Canonical: P15085 (Residues: 111-418; Coverage: 76%)
Gene names: CPA, CPA1
Sequence domains: Zinc carboxypeptidase
Structure domains: Zn peptidases

Ligands and Environments

2 bound ligands:
Ligand TJE 2 x TJE
Ligand ZN 2 x ZN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALBA BEAMLINE XALOC
Spacegroup: P212121
Unit cell:
a: 46.121Å b: 84.109Å c: 158.195Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.16 0.158 0.183
Expression system: Komagataella pastoris

Quick links

Citations

1 citations in other articles

Practical Synthesis of Phosphinic Dipeptides by Tandem Esterification of Aminophosphinic and Acrylic Acids under Silylating Conditions.
Kokkala et al. (2022)

1 mention without citation

Phosphinic Peptides as Tool Compounds for the Study of Pharmacologically Relevant Zn-Metalloproteases.
Georgiadis et al. (2022)