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 |
134
|
sequence length |
465
|
structure length |
465
|
Chain Sequence |
SNGQITAVIGAVVDVQFEDQLPPILNALEVQGRSPRLILEVAQHLGENTVRTIAMDGTEGLVRGQNVLDTGAPIKIPVGPETLGRIMNVIGEPIDERGPIVTDKFAAIHADAPEFVEMSVQQEILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELINNVAKAHGGYSVFAGVGERTREGNDLYHEMIESGVISLKDKTSKVALVYGQMNEPPGARARVALTGLTVAEYFRDQEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGTMQERITTTKKGSITSVQAIYVPADDLTDPAPATTFAHLDATTVLSRAIAELGIYPAVDPLDSTSRILDPNIIGEEHYNIARGVQKILQDYKSLQDIIAILGMDELSEEDKLIVSRARKIQRFLSQPFQVAEVFTGHAGKLVPIKDTIKGFKMILNGELDHLPEVAFYMVGPIEEVVAKAEKI
|
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 |
Cryo-EM structure of the brine shrimp mitochondrial ATP synthase suggests an inactivation mechanism for the ATP synthase leak channel.
pubmed doi rcsb |
| molecule keywords |
ATP synthase subunit c
|
| molecule tags |
Membrane protein
|
| total genus |
134
|
| structure length |
465
|
| sequence length |
465
|
| chains with identical sequence |
E, F
|
| ec nomenclature |
ec
7.1.2.2: H(+)-transporting two-sector ATPase. |
| pdb deposition date | 2024-03-12 |
Image from the rcsb pdb (www.rcsb.org)
#similar chains in the Genus database (?% sequence similarity) ...loading similar chains, please wait... #similar chains, but unknotted ...loading similar chains, please wait... #similar chains in the pdb database (?% sequence similarity) ...loading similar chains, please wait...
