The genus trace: a function that shows values of genus (vertical axis) for subchains spanned between the first residue, and all other residues (shown on horizontal axis). The number of the latter residue and the genus of a given subchain are shown interactively.
Total Genus |
172
|
sequence length |
487
|
structure length |
487
|
Chain Sequence |
DLEETGRVLSIGDGIARVHGLRNVQAEEMVEFSSGLKGMSLNLEPDNVGVVVFGNDKLIKEGDIVKRTGAIVDVPVGEELLGRVVDALGNAIDGKGPIGSKARRRVGLKAPGIIPRISVREPMQTGIKAVDSLVPIGRGQRELIIGDRQTGKTSIAIDTIINQKRFNDGTDEKKKLYCIYVAIGQKRSTVAQLVKRLTDADAMKYTIVVSATASDAAPLQYLAPYSGCSMGEYFRDNGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKMNDAFGGGSLTALPVIETQAGDVSAYIPTNVISITDGQIFLETELFYKGIRPAINVGLSVSRVGSAAQTRAMKQVAGTMKLELAQYREVAAFAQFGSDLDAATQQLLSRGVRLTELLKQGQYSPMAIEEQVAVIYAGVRGYLDKLEPSKITKFENAFLSHVISQHQALLGKIRTDGKISEESDAKLKEIVTNFLAGFEA
|
The genus matrix. At position (x,y) a genus value for a subchain spanned between x’th and y’th residue is shown. Values of the genus are represented by color, according to the scale given on the right.
After clicking on a point (x,y) in the genus matrix above, a subchain from x to y is shown in color.
publication title |
Structure at 2.8 A resolution of F1-ATPase from bovine heart mitochondria.
pubmed doi rcsb |
molecule tags |
Atp phosphorylase
|
molecule keywords |
BOVINE MITOCHONDRIAL F1-ATPASE
|
total genus |
172
|
structure length |
487
|
sequence length |
487
|
chains with identical sequence |
B, C
|
ec nomenclature | |
pdb deposition date | 1996-03-13 |
chain | Pfam Accession Code | Pfam Family Identifier | Pfam Description |
---|---|---|---|
A | PF00006 | ATP-synt_ab | ATP synthase alpha/beta family, nucleotide-binding domain |
A | PF00306 | ATP-synt_ab_C | ATP synthase alpha/beta chain, C terminal domain |
A | PF02874 | ATP-synt_ab_N | ATP synthase alpha/beta family, beta-barrel domain |
cath code
| Class | Architecture | Topology | Homology | Domain |
---|---|---|---|---|---|
Mainly Alpha | Up-down Bundle | Lysin | Lysin | ||
Mainly Beta | Beta Barrel | Elongation Factor Tu (Ef-tu); domain 3 | Elongation Factor Tu (Ef-tu); domain 3 | ||
Alpha Beta | 3-Layer(aba) Sandwich | Rossmann fold | P-loop containing nucleotide triphosphate hydrolases |