SCOPe 2.06: Domain d1isyb2: 1isy B:501-803

Lineage for d1isyb2 (1isy B:501-803)

1. Root: SCOPe 2.06

2. Class c: Alpha and beta proteins (a/b) [51349] (148 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] (15 families)

5. Family c.1.8.3: beta-glycanases [51487] (27 proteins)
   consist of a number of sequence families

6. Protein Xylanase A, catalytic core [51514] (8 species)

7. Species Streptomyces olivaceoviridis [TaxId:1921] [51519] (12 PDB entries)
   Uniprot Q7SI98
   N-terminal domain; fused with a ricin A-like beta-trefoil domain

8. Domain d1isyb2: 1isy B:501-803 [66356]
   Other proteins in same PDB: d1isya1, d1isyb1
   complexed with bgc

Details for d1isyb2

PDB Entry: 1isy, 2.1 Å

PDB Description: crystal structure of xylanase from streptomyces olivaceoviridis e-86 complexed with glucose

PDB Compounds: (B:) endo-1,4-beta-D-xylanase

SCOPe Domain Sequences for d1isyb2:

Sequence; same for both SEQRES and ATOM records:

>d1isyb2 c.1.8.3 (B:501-803) Xylanase A, catalytic core {Streptomyces olivaceoviridis [TaxId: 1921]}
aestlgaaaaqsgryfgtaiasgklgdsayttiasrefnmvtaenemkidatepqrgqfn
fsagdrvynwavqngkqvrghtlawhsqqpgwmqslsgstlrqamidhingvmghykgki
aqwdvvneafsddgsggrrdsnlqrtgndwievafrtaraadpaaklcyndynienwtwa
ktqgvynmvrdfkqrgvpidcvgfqshfnsgspynsnfrttlqnfaalgvdvaiteldiq
gassstyaavtndclavsrclgitvwgvrdtdswrsgdtpllfngdgskkaaytavlnal
ngg

Timeline for d1isyb2:

• d1isyb2 first appeared in SCOP 1.59
  
• d1isyb2 appears in SCOPe 2.05
  
• d1isyb2 appears in SCOPe 2.07
  
• d1isyb2 appears in the current release, SCOPe 2.08