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Structure paper

TitleCrystal structures of the naturally fused CS and cytochrome b5reductase (b5R) domains of Ncb5or reveal an expanded CS fold, extensive CS-b5R interactions and productive binding of the NAD(P)+nicotinamide ring.
Journal, issue, pagesActa Crystallogr D Struct Biol, Vol. 75, Page 628-638, Year 2019
Publish dateOct 24, 2018 (structure data deposition date)
AuthorsBenson, D.R. / Lovell, S. / Mehzabeen, N. / Galeva, N. / Cooper, A. / Gao, P. / Battaile, K.P. / Zhu, H.
External linksActa Crystallogr D Struct Biol / PubMed:31282472
MethodsX-ray diffraction
Resolution2.05 - 2.15 Å
Structure data

PDB-6mv1:
2.15A resolution structure of the CS-b5R domains of human Ncb5or (NAD+ form)
Method: X-RAY DIFFRACTION / Resolution: 2.15 Å

PDB-6mv2:
2.05A resolution structure of the CS-b5R domains of human Ncb5or (NADP+ form)
Method: X-RAY DIFFRACTION / Resolution: 2.05 Å

Chemicals

ChemComp-FAD:
FLAVIN-ADENINE DINUCLEOTIDE / FAD*YM

ChemComp-NAD:
NICOTINAMIDE-ADENINE-DINUCLEOTIDE / NAD*YM

ChemComp-HOH:
WATER

ChemComp-NAP:
NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE

Source
  • homo sapiens (human)
KeywordsOXIDOREDUCTASE / NCB5OR / ELECTRON TRANSFER / REDOX / HEME / ENDOPLASMIC RETICULUM / FAD / FLAVOPROTEIN / IRON / METAL-BINDING / NAD

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