Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

ChainsTypeFamily Name Domain Identifier Family IdentifierProvenance Source (Version)
ASCOP2B SuperfamilyThioredoxin-like 8057903 3000031 SCOP2B (2022-06-29)
BSCOP2B SuperfamilyThioredoxin-like 8057903 3000031 SCOP2B (2022-06-29)
CSCOP2B SuperfamilyThioredoxin-like 8057903 3000031 SCOP2B (2022-06-29)
DSCOP2B SuperfamilyThioredoxin-like 8057903 3000031 SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

ChainsFamily NameDomain Identifier ArchitecturePossible HomologyHomologyTopologyFamilyProvenance Source (Version)
AAhpC-TSA_1e3tb2A1 A: a+b three layersX: Thioredoxin-likeH: Thioredoxin-like (From Topology)T: Thioredoxin-likeF: AhpC-TSA_1ECOD (1.6)
BAhpC-TSA_1e3tb2B1 A: a+b three layersX: Thioredoxin-likeH: Thioredoxin-like (From Topology)T: Thioredoxin-likeF: AhpC-TSA_1ECOD (1.6)
CAhpC-TSA_1e3tb2C1 A: a+b three layersX: Thioredoxin-likeH: Thioredoxin-like (From Topology)T: Thioredoxin-likeF: AhpC-TSA_1ECOD (1.6)
DAhpC-TSA_1e3tb2D1 A: a+b three layersX: Thioredoxin-likeH: Thioredoxin-like (From Topology)T: Thioredoxin-likeF: AhpC-TSA_1ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Protein Family Annotation Pfam Database Homepage

ChainsAccessionNameDescriptionCommentsSource
A, B, C, D
PF00578AhpC/TSA family (AhpC-TSA)AhpC/TSA familyThis family contains proteins related to alkyl hydroperoxide reductase (AhpC) and thiol specific antioxidant (TSA).Domain
A, B, C, D
PF10417C-terminal domain of 1-Cys peroxiredoxin (1-cysPrx_C)C-terminal domain of 1-Cys peroxiredoxinThis is the C-terminal domain of 1-Cys peroxiredoxin (1-cysPrx), a member of the peroxiredoxin superfamily which protect cells against membrane oxidation through glutathione (GSH)-dependent reduction of phospholipid hydroperoxides to corresponding al ...This is the C-terminal domain of 1-Cys peroxiredoxin (1-cysPrx), a member of the peroxiredoxin superfamily which protect cells against membrane oxidation through glutathione (GSH)-dependent reduction of phospholipid hydroperoxides to corresponding alcohols [1]. The C-terminal domain is crucial for providing the extra cysteine necessary for dimerisation of the whole molecule. Loss of the enzyme's peroxidase activity is associated with oxidation of the catalytic cysteine, upstream of this domain; and glutathionylation, presumably through its disruption of protein structure, facilitates access for GSH, resulting in spontaneous reduction of the mixed disulfide to the sulfhydryl and consequent activation of the enzyme [2]. The domain is associated with family AhpC-TSA, Pfam:PF00578, which carries the catalytic cysteine.
Domain

Protein Modification Annotation

Modified Residue(s)
ChainResidue(s)Description
A, B, C, D
CSD Parent Component: CYS

RESIDAA0262

PSI-MOD :  L-cysteine sulfinic acid MOD:00267