2XQT

Microscopic rotary mechanism of ion translocation in the Fo complex of ATP synthases


Domain Annotation: ECOD Classification ECOD Database Homepage

ChainsFamily NameDomain Identifier ArchitecturePossible HomologyHomologyTopologyFamilyProvenance Source (Version)
AATP-synt_Ce2xqtA1 A: extended segmentsX: F1F0 ATP synthase subunit C (From Topology)H: F1F0 ATP synthase subunit C (From Topology)T: F1F0 ATP synthase subunit CF: ATP-synt_CECOD (1.6)
CATP-synt_Ce2xqtC1 A: extended segmentsX: F1F0 ATP synthase subunit C (From Topology)H: F1F0 ATP synthase subunit C (From Topology)T: F1F0 ATP synthase subunit CF: ATP-synt_CECOD (1.6)
BATP-synt_Ce2xqtB1 A: extended segmentsX: F1F0 ATP synthase subunit C (From Topology)H: F1F0 ATP synthase subunit C (From Topology)T: F1F0 ATP synthase subunit CF: ATP-synt_CECOD (1.6)
DATP-synt_Ce2xqtD1 A: extended segmentsX: F1F0 ATP synthase subunit C (From Topology)H: F1F0 ATP synthase subunit C (From Topology)T: F1F0 ATP synthase subunit CF: ATP-synt_CECOD (1.6)
EATP-synt_Ce2xqtE1 A: extended segmentsX: F1F0 ATP synthase subunit C (From Topology)H: F1F0 ATP synthase subunit C (From Topology)T: F1F0 ATP synthase subunit CF: ATP-synt_CECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Protein Modification Annotation

Modified Residue(s)
ChainResidue(s)Description
A, B, C, D, E
FME Parent Component: MET

RESIDAA0021 , AA0566

PSI-MOD :  N-formyl-L-methionine residue MOD:00030 , N-formyl-L-methionine (Met) MOD:00482 , N-[(L-histidin-1'-yl)methyl]-L-methionine (fMet) MOD:01890 , N-[(L-histidin-1'-yl)methyl]-L-methionine (Met) MOD:01891