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5H82

HETEROYOHIMBINE SYNTHASE THAS2 FROM CATHARANTHUS ROSEUS - APO FORM

Summary for 5H82
Entry DOI10.2210/pdb5h82/pdb
Descriptorheteroyohimbine synthase THAS2, ZINC ION (3 entities in total)
Functional Keywordsheteroyohimbine synthase, medium chain dehydrogenase/reductase, nadp+ dependent enzyme, zinc binding site, oxidoreductase
Biological sourceCatharanthus roseus (Madagascar periwinkle)
Total number of polymer chains2
Total formula weight85499.35
Authors
Stavrinides, A.,Tatsis, E.C.,Caputi, L.,Foureau, E.,Stevenson, C.E.M.,Lawson, D.M.,Courdavault, V.,O'Connor, S.E. (deposition date: 2015-12-23, release date: 2016-07-27, Last modification date: 2024-01-10)
Primary citationStavrinides, A.,Tatsis, E.C.,Caputi, L.,Foureau, E.,Stevenson, C.E.,Lawson, D.M.,Courdavault, V.,O'Connor, S.E.
Structural investigation of heteroyohimbine alkaloid synthesis reveals active site elements that control stereoselectivity.
Nat Commun, 7:12116-12116, 2016
Cited by
PubMed: 27418042
DOI: 10.1038/ncomms12116
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.05 Å)
Structure validation

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