Class c: Alpha and beta proteins (a/b) [51349] (148 folds) |
Fold c.111: Activating enzymes of the ubiquitin-like proteins [69571] (1 superfamily) 3 layers: a/b/a; mixed beta-sheet of 8 strands, order 32145678; strands 6 and 8 are antiparallel to the rest |
Superfamily c.111.1: Activating enzymes of the ubiquitin-like proteins [69572] (3 families) transfer adenylyl group to the C-terminal carboxyl group of the ubiquitin and MoaD/ThiS-related proteins the ATP nucleotide-binding site is similar to that of the NAD-binding Rossmann-folds |
Family c.111.1.2: Ubiquitin activating enzymes (UBA) [89763] (3 proteins) the common fold is elaborated with additional (sub)domains |
Protein Amyloid beta precursor protein-binding protein 1, APPBP1 [89766] (1 species) a subunit of the heterodimeric E1 enzyme for NEDD8; contains a large insertion (residues 170-487) that can be divided into 3 units similar to the UBA3 insertion |
Species Human (Homo sapiens) [TaxId:9606] [89767] (10 PDB entries) Uniprot Q13564 |
Domain d1ngva_: 1ngv A: [302766] Other proteins in same PDB: d1ngvb_, d1ngvd_ automated match to d1tt5a_ complexed with zn |
PDB Entry: 1ngv (more details), 2.6 Å
SCOPe Domain Sequences for d1ngva_:
Sequence; same for both SEQRES and ATOM records: (download)
>d1ngva_ c.111.1.2 (A:) Amyloid beta precursor protein-binding protein 1, APPBP1 {Human (Homo sapiens) [TaxId: 9606]} kllkeqkydrqlrlwgdhgqealesahvclinatatgteilknlvlpgigsftiidgnqv sgedagnnfflqrssigknraeaameflqelnsdvsgsfveespenlldndpsffcrftv vvatqlpestslrladvlwnsqipllicrtyglvgymriiikehpvieshpdnaledlrl dkpfpelrehfqsydldhmekkdhshtpwiviiakylaqwysetngripktykekedfrd lirqgilknengapedeenfeeaiknvntalnttqipssiedifnddrcinitkqtpsfw ilaralkefvakegqgnlpvrgtipdmiadsgkyiklqnvyrekakkdaaavgnhvakll qsigqapesisekelkllcsnsaflrvvrcrslaeeygldtinkdeiissmdnpdneivl ylmlravdrfhkqqgrypgvsnyqveedigklkscltgflqeyglsvmvkddyvhefcry gaaephtiaaflggaaaqevikiitkqfvifnntyiysgmsqtsatfql
Timeline for d1ngva_: