1gp5 Summary

pdbe.org/1gp5
spacer

Anthocyanidin synthase from Arabidopsis thaliana complexed with trans-dihydroquercetin

The structure was published by Wilmouth, R.C., Turnbull, J.J., Welford, R.W.D., Clifton, I.J., Prescott, A.G., and Schofield, C.J., in 2002 in a paper entitled "Structure and Mechanism of Anthocyanidin Synthase from Arabidopsis Thaliana." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.2 Å and deposited in 2001.

The experimental data on which the structure is based was also deposited.

The PDB entry contains the structure of LEUCOANTHOCYANIDIN DIOXYGENASE. This molecule has the UniProt identifier Q96323 (LDOX_ARATH)search. The sample contained 356 residues which is 100% of the natural sequence. Out of 356 residues 340 were observed and are deposited in the PDB.

It also contains one or more heterogenic compounds (e.g., ligands, co-factors, ions, modified amino acids, etc.); see here for a complete list.

The molecule is most likely monomeric.

The following tables show cross-reference information to other databases (to obtain a list of all PDB entries sharing the same property or classification, click on the magnifying glass icon):


Chain Name UniProt Name of source organism % of UniProt sequence present in the sample Residues in the sample molecules % of residues observed
A LEUCOANTHOCYANIDIN DIOXYGENASE Q96323 (1-356) (LDOX_ARATH)search Arabidopsis thalianasearch 100% 356 97%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
Q96323 (1 - 356) LEUCOANTHOCYANIDIN DIOXYGENASE Arabidopsis thaliana

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A (Q96323) Penicillin synthase-likesearch B-lactam Antibiotic, Isopenicillin N Synthase; Chainsearch PF03171: 2OG-Fe(II) oxygenase superfamilysearch, PF14226: non-haem dioxygenase in morphine synthesis N-terminalsearch

Chain ID Molecular function (GO) Biological process (GO)
A (Q96323) L-ascorbic acid bindingsearch oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, 2-oxoglutarate as one donor, and incorporation of one atom each of oxygen into both donorssearch oxidoreductase activitysearch leucocyanidin oxygenase activitysearch metal ion bindingsearch dioxygenase activitysearch flavonoid biosynthetic processsearch oxidation-reduction processsearch anthocyanin-containing compound biosynthetic processsearch response to woundingsearch vacuole organizationsearch response to jasmonic acidsearch proanthocyanidin biosynthetic processsearch

Chain InterPro annotation
A Oxoglutarate/iron-dependent dioxygenasesearch Non-haem dioxygenase N-terminal domainsearch Isopenicillin N synthase-likesearch