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Literature summary extracted from

  • Kumari, V.; Kumar, V.; Bhalla, T.C.
    Functional interpretation and structural insights of Arabidopsis lyrata cytochrome P450 CYP71A13 involved in auxin synthesis (2015), Bioinformation, 11, 330-335 .
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
4.8.1.3 homology modeling of structure. The heme resides between H-helix and J-helix in the hydrophobic pocket, where residues Gly305 and Thr308, 311 of the H-helix are involved in its stabilization. Substrate indole-3-acetaldoxime is tightly fitted into the substrate. The smaller size of the substrate binding pocket is due to the bulkiness of the two amino acid residues Phe182 and Trp315 pointing into the substrate binding cavity. The heme tethers the substrate during catalysis Arabidopsis lyrata subsp. lyrata

Organism

EC Number Organism UniProt Comment Textmining
4.8.1.3 Arabidopsis lyrata subsp. lyrata D7LC87
-
-

Subunits

EC Number Subunits Comment Organism
4.8.1.3 ? x * 57000, calculated from sequence Arabidopsis lyrata subsp. lyrata

Synonyms

EC Number Synonyms Comment Organism
4.8.1.3 ARALYDRAFT_481994
-
 Arabidopsis lyrata subsp. lyrata
4.8.1.3 CYP71A13
-
 Arabidopsis lyrata subsp. lyrata

Cofactor

EC Number Cofactor Comment Organism Structure
4.8.1.3 heme
-
 Arabidopsis lyrata subsp. lyrata