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EBI PDBe PDBeView

PDBe Entry: 1i7p view

CRYSTAL STRUCTURE OF RAT B5R IN COMPLEX WITH FAD
Summary
Header OXYGEN STORAGE/TRANSPORTsearch
Method X-RAY DIFFRACTION
Experiment Resolution: 2.0 Å, R-factor: 21.5%, Free R-factor: 24.44%, Spacegroup: P 21 21 21
Released 12/12/2001, deposition: 10/03/2001, last revision: 24/02/2009
Authors Bewley, M.C.search; Marohnic, C.C.search; Barber, M.J.search
Primary citation The structure and biochemistry of NADH-dependent cytochrome b5 reductase are now consistent.
BIOCHEMISTRYsearch vol:40, pag:13574-13582 (2001) [PubMed ID 11695905 ]search
Keywords ELECTRON TRANSPORTsearch, HEMOGLOBINEMIAsearch, ERYTHROCYTE FUNCTIONsearch, FAD-BINDINGsearch, NADH-BINDINGsearch, OXYGEN STORAGE/TRANSPORT COMPLEXsearch
EC 1.6.2.2 ExPASy BRENDA search (A)
Organism Rattus norvegicus(Norway rat) 10116search(A)
UniProt NADH-cytochrome b5 reductase 3 (EC 1.6.2.2) (Cytochrome b5 reductase) (B5R) (Diaphorase-1) [Contains: NADH-cytochrome b5 reductase 3 membrane-bound form; NADH-cytochrome b5 reductase 3 soluble form] P20070search (A)
Solvent A
Related entries 1ndh, 1ib0
Polymers
Id Name Type UniProt Residues Observed
A NADH-CYTOCHROME B5 REDUCTASE Protein P20070 (NB5R3_RAT)search
 274 99%
Heterogens
Id Name Ligands
A FLAVIN-ADENINE DINUCLEOTIDE FAD search
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