SCOP 1.73: Domain d1byca_: 1byc A:

Lineage for d1byca_ (1byc A:)

1. Root: SCOP 1.73

2. Class c: Alpha and beta proteins (a/b) [51349] (141 folds)

3. 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

4. Superfamily c.1.8: (Trans)glycosidases [51445] (14 families)

5. Family c.1.8.1: Amylase, catalytic domain [51446] (24 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

6. Protein beta-Amylase [51481] (3 species)
   Common fold covers whole protein structure

7. Species Soybean (Glycine max) [TaxId:3847] [51482] (19 PDB entries)

8. Domain d1byca_: 1byc A: [28793]
   complexed with glc, so4

Details for d1byca_

PDB Entry: 1byc, 2.2 Å

PDB Description: crystal structures of soybean beta-amylase reacted with beta-maltose and maltal: active site components and their apparent role in catalysis

PDB Compounds: (A:) beta-amylase

SCOP Domain Sequences for d1byca_:

Sequence; same for both SEQRES and ATOM records:

>d1byca_ c.1.8.1 (A:) beta-Amylase {Soybean (Glycine max) [TaxId: 3847]}
snmllnyvpvyvmlplgvvnvdnvfedpdglkeqllqlraagvdgvmvdvwwgiielkgp
kqydwrayrslfqlvqecgltlqaimsfhqcggnvgdivnipipqwvldigesnhdifyt
nrsgtrnkeyltvgvdnepifhgrtaieiysdymksfrenmsdflesgliidievglgpa
gelrypsypqsqgwefprigefqcydkylkadfkaavaraghpewelpddagkyndvpes
tgffksngtyvtekgkffltwysnkllnhgdqildeankaflgckvklaikvsgihwwyk
venhaaeltagyynlndrdgyrpiarmlsrhhailnftclemrdseqpsdaksgpqelvq
qvlsggwredirvagenalprydataynqiilnakpqgvnnngppklsmfgvtylrlsdd
llqksnfnifkkfvlkmhadqdycanpqkynhaitplkpsapkipievlleatkptlpfp
wlpetdmkvdg

Timeline for d1byca_:

• d1byca_ first appeared (with stable ids) in SCOP 1.55, called d1byc__
  
• d1byca_ was called d1byc__ in SCOP 1.71
  
• d1byca_ appears in SCOP 1.75
  
• d1byca_ appears in the current release, SCOPe 2.08