Sulfhydryl oxidase
From Proteopedia
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==3D structures of sulfhydryl oxidase== | ==3D structures of sulfhydryl oxidase== | ||
| - | + | Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}} | |
===Erv2p=== | ===Erv2p=== | ||
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===Erv1=== | ===Erv1=== | ||
| - | [[4e0h]] – ySOX FAD-binding domain<br /> | + | [[4e0h]], [[3w4y]] – ySOX FAD-binding domain<br /> |
[[4e0i]] – ySOX FAD-binding domain (mutant) | [[4e0i]] – ySOX FAD-binding domain (mutant) | ||
Revision as of 09:58, 22 October 2013
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 SOX is involved in the biogenesis of Fe/S clusters. ALR is a SOX augmenter of liver regeneration. QSOX is a quiescin SOX. QSOX contain thioredoxin domain, helix-rich domain and FAD-binding domain Erv/ALR.
Contents |
3D structures of sulfhydryl oxidase
Updated on 22-October-2013
Erv2p
1jr8, 1jra – ySOX protease-resistant domain – yeast
Erv1
4e0h, 3w4y – ySOX FAD-binding domain
4e0i – ySOX FAD-binding domain (mutant)
Erv1p
2hj3 – SOX – Arabidopsis thaliana
Erv
3p0k, 3qzy – SOX – Autographa californica nucleopolyhedrovirus
ASFV
3gwl – SOX residues 1-103 – African swine fever virus
QSOX1
3lli, 3llk – hSOX-1 residues 286-546 – human
3q6o - hSOX-1 residues 33-272
3t58, 3t59 - mSOX-1 residues 36-550 (mutant) - mouse
ALR
3mbg, 3tk0 – hALR residues 81-205
3u2l, 3u2m, 3u5s – hALR (mutant)
3r7c - ALR - rat
FAD-linked SOX
3td7 – SOX (mutant) – Acanthamoeba polyphaga minivirus
