This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.


Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


NADH-cytochrome b5 reductase

From Proteopedia

Jump to: navigation, search

Pig b5R 3 complex with FAD and glycerol (PDB code 5gv7)

Drag the structure with the mouse to rotate

3D structures of NADH-cytochrome b5 reductase

Updated on 11-July-2023

1umk, 7thg, 7two - hb5R3 + FAD - human
7tnv, 7tsw - hb5R3 (mutant) + FAD
1umk - hb5R + FAD - human
3w5h, 5gv7, 5gv8, 1ndh, 3w2e, 3w2f, 3w2g, 3w2h, 3w2i - b5R 3 + FAD + NAD - pig
1i7p - rb5R soluble domain + FAD - rat
1qx4 - rb5R soluble domain (mutant) + FAD
1ib0 - rb5R soluble domain + FAD + NAD
7rom - b5R (mutant) + FAD - yeast
2eix - b5R + FAD - Physarum polycephalum

References

  1. Bando S, Takano T, Yubisui T, Shirabe K, Takeshita M, Nakagawa A. Structure of human erythrocyte NADH-cytochrome b5 reductase. Acta Crystallogr D Biol Crystallogr. 2004 Nov;60(Pt 11):1929-34. Epub 2004, Oct 20. PMID:15502298 doi:10.1107/S0907444904020645
  2. Aalfs CM, Salieb-Beugelaar GB, Wanders RJ, Mannens MM, Wijburg FA. A case of methemoglobinemia type II due to NADH-cytochrome b5 reductase deficiency: determination of the molecular basis. Hum Mutat. 2000;16(1):18-22. doi:, 10.1002/1098-1004(200007)16:1<18::AID-HUMU4>3.0.CO;2-N. PMID:10874300 doi:<18::AID-HUMU4>3.0.CO;2-N http://dx.doi.org/10.1002/1098-1004(200007)16:1<18::AID-HUMU4>3.0.CO;2-N
  3. Sacco JC, Trepanier LA. Cytochrome b5 and NADH cytochrome b5 reductase: genotype-phenotype correlations for hydroxylamine reduction. Pharmacogenet Genomics. 2010 Jan;20(1):26-37. doi: 10.1097/FPC.0b013e3283343296. PMID:19997042 doi:http://dx.doi.org/10.1097/FPC.0b013e3283343296

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel

Personal tools