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4ka8

X-ray diffraction
1.9Å resolution

Structure of Organellar OligoPeptidase

Released:
Model geometry
Fit model/data

Function and Biology Details

Reaction catalysed:
Hydrolysis of oligopeptides, with broad specificity. Gly or Ala commonlyoccur as P1 or P1' residues, but more distant residues are alsoimportant, as is shown by the fact that Z-Gly-Pro-Gly-|-Gly-Pro-Ala iscleaved, but not Z-(Gly)(5).
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-188215 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Organellar oligopeptidase A, chloroplastic/mitochondrial Chain: A
Molecule details ›
Chain: A
Length: 714 amino acids
Theoretical weight: 80.27 KDa
Source organism: Arabidopsis thaliana
Expression system: Escherichia coli
UniProt:
  • Canonical: Q94AM1 (Residues: 83-791; Coverage: 90%)
Gene names: At5g65620, K21L13.14, OOP, PRD1, TOP1
Sequence domains:
Structure domains: Neurolysin; domain 3

Ligands and Environments

No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: SLS BEAMLINE X06SA
Spacegroup: P212121
Unit cell:
a: 71.817Å b: 101.339Å c: 132.908Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.193 0.191 0.218
Expression system: Escherichia coli