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1F2V

CRYSTAL STRUCTURE ANALYSIS OF PRECORRIN-8X METHYLMUTASE OF AEROBIC VITAMIN B12 SYNTHESIS

Summary for 1F2V
Entry DOI10.2210/pdb1f2v/pdb
DescriptorPRECORRIN-8X METHYLMUTASE (2 entities in total)
Functional Keywordsalpha-beta wind, doubly wound sheet, isomerase
Biological sourcePseudomonas denitrificans
Total number of polymer chains1
Total formula weight23217.51
Authors
Shipman, L.W.,Li, D.,Roessner, C.A.,Scott, A.I.,Sacchettini, J.C. (deposition date: 2000-05-29, release date: 2001-07-18, Last modification date: 2024-02-07)
Primary citationShipman, L.W.,Li, D.,Roessner, C.A.,Scott, A.I.,Sacchettini, J.C.
Crystal structure of precorrin-8x methyl mutase.
Structure, 9:587-596, 2001
Cited by
PubMed Abstract: The crystal structure of precorrin-8x methyl mutase (CobH), an enzyme of the aerobic pathway to vitamin B12, provides evidence that the mechanism for methyl migration can plausibly be regarded as an allowed [1,5]-sigmatropic shift of a methyl group from C-11 to C-12 at the C ring of precorrin-8x to afford hydrogenobyrinic acid.
PubMed: 11470433
DOI: 10.1016/S0969-2126(01)00618-9
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.1 Å)
Structure validation

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