› 8fjd

X-ray diffraction
4.46Å resolution

Structure of chlorophyllase from Triticum aestivum

Released:
DOI: 10.2210/pdb8fjd/pdb
PDB entry 8fjd coloured by chain, front view.
PDB entry 8fjd coloured by chain, side view.
PDB entry 8fjd coloured by chain, top view.
Source organism: Triticum aestivum
Primary publication:
A structure-function analysis of chlorophyllase reveals a mechanism for activity regulation dependent on disulfide bonds.
Jo M, Knapp M, Boggs DG, Brimberry M, Donnan PH, Bridwell-Rabb J
J Biol Chem 102958 (2023)
PMID: 36731794

Function and Biology Details

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-226613 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
PET hydrolase-like domain-containing protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 325 amino acids
Theoretical weight: 34.67 KDa
Source organism: Triticum aestivum
Expression system: Escherichia coli
UniProt:
  • Canonical: A0A3B6QC98 (Residues: 1-319; Coverage: 100%)
Gene name: CFC21_092079
Sequence domains: Cutinase

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-G
Spacegroup: P6522
Unit cell:
a: 197.52Å b: 197.52Å c: 96.83Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.266 0.266 0.278
Expression system: Escherichia coli

Quick links

Citations

2 citation in other articles

Leveraging a Structural Blueprint to Rationally Engineer the Rieske Oxygenase TsaM.
Tian et al. (2023)
1 more

1 mention without citation

A structure-function analysis of chlorophyllase reveals a mechanism for activity regulation dependent on disulfide bonds.
Jo et al. (2023)