1BG5

CRYSTAL STRUCTURE OF THE ANKYRIN BINDING DOMAIN OF ALPHA-NA,K-ATPASE AS A FUSION PROTEIN WITH GLUTATHIONE S-TRANSFERASE


Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

ChainsTypeFamily Name Domain Identifier Family IdentifierProvenance Source (Version)
ASCOP2B SuperfamilyGST C-terminal domain-like8037552 3000305 SCOP2B (2022-06-29)
ASCOP2B SuperfamilyThioredoxin-like8044378 3000031 SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

ChainsFamily NameDomain Identifier ArchitecturePossible HomologyHomologyTopologyFamilyProvenance Source (Version)
AF_UNCLASSIFIEDe1bg5A3 A: alpha bundlesX: Calcium ATPase transmembrane domain-related (From Homology)H: Calcium ATPase transmembrane domain-relatedT: Calcium ATPase transmembrane domain MF: F_UNCLASSIFIEDECOD (1.6)
APF14497e1bg5A1 A: alpha superhelicesX: Repetitive alpha hairpinsH: Glutathione S-transferase (GST)-C (From Topology)T: Glutathione S-transferase (GST)-CF: PF14497ECOD (1.6)
APF02798e1bg5A2 A: a+b three layersX: Thioredoxin-likeH: Thioredoxin-like (From Topology)T: Thioredoxin-likeF: PF02798ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Protein Family Annotation Pfam Database Homepage

ChainsAccessionNameDescriptionCommentsSource
PF14497Glutathione S-transferase, C-terminal domain (GST_C_3)Glutathione S-transferase, C-terminal domainThis domain is closely related to Pfam:PF00043.Domain
PF02798Glutathione S-transferase, N-terminal domain (GST_N)Glutathione S-transferase, N-terminal domainFunction: conjugation of reduced glutathione to a variety of targets. Also included in the alignment, but not GSTs: S-crystallins from squid (similarity to GST previously noted); eukaryotic elongation factors 1-gamma (not known to have GST activity a ...Function: conjugation of reduced glutathione to a variety of targets. Also included in the alignment, but not GSTs: S-crystallins from squid (similarity to GST previously noted); eukaryotic elongation factors 1-gamma (not known to have GST activity and similarity not previously recognised); HSP26 family of stress-related proteins including auxin-regulated proteins in plants and stringent starvation proteins in E. coli (not known to have GST activity and similarity not previously recognised). The glutathione molecule binds in a cleft between the N- and C-terminal domains - the catalytically important residues are proposed to reside in the N-terminal domain [1].
Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

ChainsPolymerMolecular FunctionBiological ProcessCellular Component
FUSION PROTEIN OF ALPHA-NA,K-ATPASE WITH GLUTATHIONE S-TRANSFERASE - -