Structural Classification of Proteins
Fold: Formate dehydrogenase/DMSO reductase, domains 1-3
contains of two similar intertwined domains related by pseudo dyad; duplication
core: 3 layers: a/b/a; parallel beta-sheet of 5 strands, order 32451
Lineage:
Root:
scop
Class:
Alpha and beta proteins (a/b)
[51349]
Mainly parallel beta sheets (beta-alpha-beta units)
Fold:
Formate dehydrogenase/DMSO reductase, domains 1-3
[53705]
contains of two similar intertwined domains related by pseudo dyad; duplication
core: 3 layers: a/b/a; parallel beta-sheet of 5 strands, order 32451
Superfamilies:
Formate dehydrogenase/DMSO reductase, domains 1-3
[53706] (1)
molybdopterine enzyme
uperfamily
Formate dehydrogenase/DMSO reductase, domains 1-3
[53707] (12)
domain 1 (residues 1-55) binds Fe4S4 cluster in FDH but not DMSO reductase
Dimethylsulfoxide reductase (DMSO reductase) [53708]
Rhodobacter sphaeroides
[TaxId: 1063]
[53709] (1)
Rhodobacter capsulatus
[TaxId: 1061]
[53710] (10)
Formate dehydrogenase H [53711]
Escherichia coli
[TaxId: 562]
[53712] (4)
Formate dehydrogenase N, alpha subunit [75317]
Escherichia coli
[TaxId: 562]
[75318] (2)
Tungsten containing formate dehydrogenase, large subunit [82536]
Desulfovibrio gigas
[TaxId: 879]
[82537] (1)
Trimethylamine N-oxide reductase [53713]
Shewanella massilia
[TaxId: 76854]
[53714] (1)
Arsenite oxidase large subunit [53715]
Alcaligenes faecalis
[TaxId: 511]
[53716] (2)
Periplasmic nitrate reductase alpha chain [53717]
Desulfovibrio desulfuricans
[TaxId: 876]
[53718] (8)
dissimilatory nitrate reductase (NAP)
Rhodobacter sphaeroides
[TaxId: 1063]
[102672] (1)
Respiratory nitrate reductase 1 alpha chain [102673]
Escherichia coli
[TaxId: 562]
[102674] (7)
SQ
P09152
Transhydroxylase alpha subunit, AthL [110729]
Pelobacter acidigallici
[TaxId: 35816]
[110730] (6)
SQ
P80563
NADH-quinone oxidoreductase chain 3, Nqo3 [142751]
Thermus thermophilus
[TaxId: 274]
[142752] (4)
SQ
Q56223
247-685
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Generated from scop database 1.75 with scopm 1.101 on Wed Jun 3 10:42:06 2009
Copyright
© 1994-2009 The scop authors / scop@mrc-lmb.cam.ac.uk