Structural Classification of Proteins
Family: Ferredoxin reductase FAD-binding domain-like
coupled with a NADP-binding domain of alpha/beta class
Lineage:
Root:
scop
Class:
All beta proteins
[48724]
Fold:
Reductase/isomerase/elongation factor common domain
[50412]
barrel, closed; n=6, S=10; greek-key
Superfamily:
Riboflavin synthase domain-like
[63380]
uperfamily
Family:
Ferredoxin reductase FAD-binding domain-like
[63381]
coupled with a NADP-binding domain of alpha/beta class
Protein Domains:
Ferredoxin reductase (flavodoxin reductase) N-terminal domain [50415]
Spinach (Spinacia oleracea)
[TaxId: 3562]
[50416] (7)
1fnd
complexed with a2p, fad, so4
region a:19-154
[25626]
1fnb
complexed with fad, po4, so4
region a:19-154
[25628]
1bx1
complexed with fad, po4, so4; mutant
region a:19-154
[25629]
1bx0
complexed with fad, po4, so4; mutant
region a:19-154
[25630]
1fnc
complexed with a2p, fda, so4
region a:19-154
[25627]
1frq
complexed with fad, po4, so4; mutant
region a:19-154
[25632]
1frn
complexed with fad, po4, so4; mutant
region a:19-154
[25631]
Garden pea (Pisum sativum)
[TaxId: 3888]
[50417] (4)
1qfz
complexed with fad, ndp, so4; mutant
region a:1-153
[25633]
region b:514-653
[25634]
1qfy
complexed with fad, nap, so4; mutant
region a:1-153
[25635]
region b:514-653
[25636]
1qga
complexed with fad, nap, so4; mutant
region a:1-153
[25637]
region b:514-653
[25638]
1qg0
complexed with fad
region a:13-153
[25639]
region b:1013-1153
[25640]
Paprika (Capsicum annuum)
[TaxId: 4072]
[50418] (1)
1sm4
complexed with fad, po4
region a:67-207
[98913]
region b:1067-1207
[98915]
Maize (Zea mays), leaf isoform
[TaxId: 4577]
[50419] (2)
1gaw
complexed with fad
region a:11-156
[25643]
region b:10-156
[25644]
1gaq
complexed with fad, fes
region a:19-156
[25645]
region c:19-156
[25646]
Maize (Zea mays), root isoform
[TaxId: 4577]
[63786] (1)
1jb9
complexed with fad
region a:6-162
[62840]
Cyanobacterium (Anabaena sp.), pcc 7119
[TaxId: 1167]
[50420] (25)
2bmw
automatically matched to d1e62a1
complexed with fad, so4; mutant
region a:9-141
[128815]
1ogi
complexed with fad, so4; mutant
region a:9-141
[92914]
1ogj
complexed with fad, so4; mutant
region a:9-141
[92916]
1w34
automatically matched to d1e62a1
complexed with fad, so4; mutant
region a:9-141
[120620]
1qgy
complexed with fad, so4; mutant
region a:9-141
[96344]
1que
complexed with fad, so4
region a:1-141
[25647]
1w35
automatically matched to d1e62a1
complexed with fad, so4; mutant
region a:9-141
[120622]
1go2
complexed with fad, so4; mutant
region a:9-141
[76243]
1b2r
region a:9-141
[25648]
2bsa
automatically matched to d1ewya1
complexed with fad, nap; mutant
region a:9-141
[129078]
1qh0
complexed with fad, so4; mutant
region a:9-141
[68891]
1qgz
complexed with fad, so4; mutant
region a:9-141
[68889]
1bjk
complexed with fad, so4; mutant
region a:9-141
[25649]
1h42
complexed with fad, so4; mutant
region a:9-141
[90606]
1e64
complexed with fad, so4; mutant
region a:9-141
[59289]
1e63
complexed with fad, so4; mutant
region a:9-141
[59287]
1gjr
complexed with fad, nap
region a:9-141
[70197]
1e62
complexed with fad, so4; mutant
region a:9-141
[59285]
1h85
complexed with fad, so4; mutant
region a:9-141
[65716]
1bqe
complexed with fad, so4; mutant
region a:9-141
[64760]
1quf
complexed with fad, nap
region a:8-141
[25650]
1gr1
complexed with fad, so4; mutant
region a:9-141
[76319]
1ewy
complexed with fad, fes
region a:1-141
[25651]
region b:1-141
[25652]
1w87
automatically matched to d1e62a1
complexed with fad, nap; mutant
region a:9-141
[120712]
1w87
automatically matched to d1e62a1
complexed with fad, nap; mutant
region b:9-141
[120714]
Escherichia coli
[TaxId: 562]
[50421] (1)
1fdr
complexed with fad; mutant
region a:2-100
[25653]
Azotobacter vinelandii
[TaxId: 354]
[50422] (1)
1a8p
complexed with fad
region a:2-100
[25654]
NAD(P)H:flavin oxidoreductase [50423]
Escherichia coli
[TaxId: 562]
[50424] (1)
1qfj
CASP3
complexed with gol
region a:1-97
[25655]
region b:1-97
[25656]
region c:1-97
[25657]
region d:1-97
[25658]
Nitrate reductase core domain [50425]
Corn (Zea mays)
[TaxId: 4577]
[50426] (3)
2cnd
complexed with fad
region a:11-124
[25659]
1cnf
complexed with adp, fad
region a:11-124
[25660]
1cne
complexed with fad; mutant
region a:11-124
[25661]
cytochrome b5 reductase [50427]
Pig (Sus scrofa), liver
[TaxId: 9823]
[50428] (1)
1ndh
complexed with fad
region a:3-125
[25662]
Rat (Rattus norvegicus)
[TaxId: 10116]
[69273] (3)
SQ
P20070
33-300
1qx4
complexed with fad; mutant
region a:33-153
[104624]
region b:33-153
[104626]
1i7p
complexed with fad
region a:29-153
[66048]
1ib0
complexed with fad, nad
region a:29-153
[66105]
Human (Homo sapiens)
[TaxId: 9606]
[117215] (1)
SQ
P00387
30-300
1umk
complexed with fad
region a:30-153
[113312]
Phthalate dioxygenase reductase [50430]
contains additional 2Fe-2S ferredoxin domain
Pseudomonas cepacia, db01
[TaxId: 292]
[50431] (1)
2pia
complexed with fes, fmn
region a:1-103
[25663]
Benzoate dioxygenase reductase [74959]
Acinetobacter sp.
[TaxId: 472]
[74960] (1)
1krh
contains 2Fe-2S cluster in the C-terminal extension
complexed with fad, fes, so4
region a:106-205
[72891]
region b:106-205
[72894]
Dihydroorotate dehydrogenase B, PyrK subunit [50433]
Lactococcus lactis, isozyme B
[TaxId: 1358]
[50434] (3)
1ep3
complexed with fad, fes, fmn
region b:2-102
[25664]
1ep1
complexed with fad, fes, fmn
region b:2-102
[25665]
1ep2
complexed with fad, fes, fmn, oro
region b:2-102
[25666]
Flavohemoglobin, central domain [50436]
contains additional globin domain
Alcaligenes eutrophus
[TaxId: 106590]
[50437] (1)
1cqx
complexed with dgg, fad, hem, na
region a:151-261
[25667]
region b:151-261
[25668]
Escherichia coli
[TaxId: 562]
[74961] (1)
1gvh
complexed with cl, fad, hem, na
region a:147-253
[70602]
Methane monooxygenase component C, MmoC [117216]
Methylococcus capsulatus
[TaxId: 414]
[117217] (1)
SQ
P22868
99-348 # structure of the N-terminal, 2Fe-2S ferredoxin domain is also known (1JQ4;
scop_sp 69669
)
1tvc
complexed with fda
region a:2-110
[112681]
Enter
search
key:
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