Class c: Alpha and beta proteins (a/b) [51349] (148 folds) |
Fold c.1: TIM beta/alpha-barrel [51350] (33 superfamilies) contains parallel beta-sheet barrel, closed; n=8, S=8; strand order 12345678 the first seven superfamilies have similar phosphate-binding sites |
Superfamily c.1.8: (Trans)glycosidases [51445] (15 families) |
Family c.1.8.1: Amylase, catalytic domain [51446] (26 proteins) members of the family may contain various insert subdomains in alpha-amylases and closer relatives this domain is usually followed by a common all-beta domain |
Protein Bacterial alpha-amylase [51447] (10 species) |
Species Chimera (Bacillus amyloliquefaciens) and (Bacillus licheniformis) [TaxId:1390] [63903] (4 PDB entries) the N-terminal 300 residues are from B. amyloliquefaciens |
Domain d1e3za2: 1e3z A:1-393 [59214] Other proteins in same PDB: d1e3za1 complexed with aci, ca, na |
PDB Entry: 1e3z (more details), 1.93 Å
SCOPe Domain Sequences for d1e3za2:
Sequence; same for both SEQRES and ATOM records: (download)
>d1e3za2 c.1.8.1 (A:1-393) Bacterial alpha-amylase {Chimera (Bacillus amyloliquefaciens) and (Bacillus licheniformis) [TaxId: 1390]} vngtlmqyfewytpndgqhwkrlqndaehlsdigitavwippaykglsqsdngygpydly dlgefqqkgtvrtkygtkselqdaigslhsrnvqvygdvvlnhkagadatedvtavevnp anrnqetseeyqikawtdfrfpgrgntysdfkwhwyhfdgadwdesrkisrifkfrgegk awdwevssengnydylmyadvdydhpdvvaetkkwgiwyanelsldgfridaakhikfsf lrdwvqavrqatgkemftvaeywqnnagklenylnktsfnqsvfdvplhfnlqaassqgg gydmrkllngtvvskhplksvtfvdnhdtqpgqslestvqtwfkplayafiltresgypq vfygdmygtkgdsqreipalkhkiepilkarkq
Timeline for d1e3za2: