5o3u

X-ray diffraction
1.86Å resolution

Structural characterization of the fast and promiscuous macrocyclase from plant - PCY1-S562A bound to Presegetalin F1

Released:

Function and Biology Details

Reaction catalysed:
Hydrolysis of --Pro-|- and to a lesser extent --Ala-|- in oligopeptides.
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
PDBe Complex ID:
PDB-CPX-123626 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Prolyl endopeptidase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 724 amino acids
Theoretical weight: 82.48 KDa
Source organism: Gypsophila vaccaria
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: R4P353 (Residues: 1-724; Coverage: 100%)
Gene name: Pcy1
Sequence domains:
Structure domains:
Putative presegetalin F1 Chains: L, M, N, O
Molecule details ›
Chains: L, M, N, O
Length: 38 amino acids
Theoretical weight: 4 KDa
Source organism: Gypsophila vaccaria
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: F6LNM3 (Residues: 1-38; Coverage: 100%)

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I24
Spacegroup: P1
Unit cell:
a: 64.86Å b: 85.82Å c: 137.87Å
α: 87.64° β: 78.32° γ: 89.52°
R-values:
R R work R free
0.194 0.193 0.223
Expression system: Escherichia coli BL21(DE3)