5dqr

X-ray diffraction
2.7Å resolution

The crystal structure of Arabidopsis 7-hydroxymethyl chlorophyll a reductase (HCAR)

Released:
Source organism: Arabidopsis thaliana
Primary publication:
Crystal Structure and Catalytic Mechanism of 7-Hydroxymethyl Chlorophyll a Reductase.
J Biol Chem 291 13349-59 (2016)
PMID: 27072131

Function and Biology Details

Reaction catalysed:
Chlorophyll a + H(2)O + 2 oxidized ferredoxin = 7(1)-hydroxychlorophyll a + 2 reduced ferredoxin + 2 H(+)
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
homo trimer (preferred)
PDBe Complex ID:
PDB-CPX-184566 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
7-hydroxymethyl chlorophyll a reductase, chloroplastic Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 437 amino acids
Theoretical weight: 49.07 KDa
Source organism: Arabidopsis thaliana
Expression system: Escherichia coli
UniProt:
  • Canonical: Q8GS60 (Residues: 26-462; Coverage: 95%)
Gene names: At1g04620, HCAR, HMCR, T1G11.13
Sequence domains:

Ligands and Environments


Cofactor: Ligand FAD 6 x FAD
1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRF BEAMLINE BL17U
Spacegroup: P32
Unit cell:
a: 89.105Å b: 89.105Å c: 273.312Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.204 0.202 0.246
Expression system: Escherichia coli