Template:STRUCTURE 3p0k
Sulfhydryl oxidase (SOX) is a flavin-dependent enzyme which catalyze the formation of disulfide bonds from thiol groups. The reaction involves the reduction of O2 to hydrogen peroxide.
- Erv1p is involved in the biogenesis of Fe/S clusters.
- ALR is a SOX augmenter of liver regeneration.
- QSOX is a quiescin SOX. QSOX contains thioredoxin domain, helix-rich domain and FAD-binding domain Erv/ALR.
3D structures of sulfhydryl oxidase3D structures of sulfhydryl oxidase
Updated on 04-September-2016
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- Sulfhydryl oxidase Erv2p
- 1jr8, 1jra – ySOX protease-resistant domain – yeast
- Sulfhydryl oxidase Erv1
- 4e0h, 3w4y – ySOX FAD-binding domain
- 4e0i – ySOX FAD-binding domain (mutant)
- Sulfhydryl oxidase Erv1p
- 2hj3 – SOX – Arabidopsis thaliana
- Sulfhydryl oxidase Erv
- 3p0k, 3qzy – SOX – Autographa californica nucleopolyhedrovirus
- Sulfhydryl oxidase ASFV
- 3gwl – SOX residues 1-103 – African swine fever virus
- Sulfhydryl oxidase QSOX1
- 3lli, 3llk – hSOX-1 residues 286-546 – human
- 3q6o - hSOX-1 residues 33-272
- 4ij3 - hSOX-1 residues 33-272 + antibody
- 3t58, 3t59 - mSOX-1 residues 36-550 (mutant) - mouse
- 4p2l - rSOX-1 residues 27-544 - rat
- Sulfhydryl oxidase ALR
- FAD-linked sulfhydryl oxidase
- 3td7 – SOX (mutant) – Acanthamoeba polyphaga minivirus