Oxidoreductase FAD-binding domain
Identifiers
SymbolFAD_binding_6
PfamPF00970
InterProIPR008333
SCOP21cne / SCOPe / SUPFAM
CDDcd00322
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary
PDB1ep1B:7-104 1ep3B:7-104 1ep2B:7-104

1cqxA:156-261 1gvhA:154-253 1krhB:120-215 2pia :11-108 2bgiA:18-114 2bgjB:18-114 1a8p :6-101 1fdrA:6-92 1cnf :365-472 2cnd :365-472 1cne :365-472 1m91A:44-151 1umkA:44-151 1ndh :15-122 1i7pA:44-151

1ib0A:44-151 1qx4B:44-151

The oxidoreductase FAD-binding domain is an evolutionary conserved protein domain. To date, the 3D-structures of the flavoprotein domain of Zea mays nitrate reductase[1] and of pig NADH:cytochrome b5 reductase[2] have been solved. The overall fold is similar to that of ferredoxin:NADP+ reductase:[3] the FAD-binding domain (N-terminal) has the topology of an anti-parallel beta-barrel, while the NAD(P)-binding domain (C-terminal) has the topology of a classical pyridine dinucleotide-binding fold (i.e. a central parallel beta-sheet flanked by 2 helices on each side).

Examples

Human genes encoding proteins containing this domain include:

References

  1. ↑ Lindqvist Y, Schneider G, Campbell WH, Lu G (1994). "Crystal structure of the FAD-containing fragment of corn nitrate reductase at 2.5 A resolution: relationship to other flavoprotein reductases". Structure. 2 (9): 809–821. doi:10.1016/s0969-2126(94)00082-4. PMID 7812715.
  2. ↑ Miki K, Nishida H, Inaka K, Yamanaka M, Kaida S, Kobayashi K (1995). "Crystal structure of NADH-cytochrome b5 reductase from pig liver at 2.4 A resolution". Biochemistry. 34 (9): 2763–2767. doi:10.1021/bi00009a004. PMID 7893687.
  3. ↑ Karplus PA, Bruns CM (1994). "Structure-function relations for ferredoxin reductase". J. Bioenerg. Biomembr. 26 (1): 89–99. doi:10.1007/BF00763221. PMID 8027025. S2CID 1004663.
This article incorporates text from the public domain Pfam and InterPro: IPR008333


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