SCOP 1.65: Domain d1isvb2: 1isv B:501-803

Lineage for d1isvb2 (1isv B:501-803)

1. Root: SCOP 1.65

2. Class c: Alpha and beta proteins (a/b) [51349] (121 folds)

3. Fold c.1: TIM beta/alpha-barrel [51350] (26 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] (9 families)

5. Family c.1.8.3: beta-glycanases [51487] (16 proteins)
   consist of a number of sequence families

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

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

8. Domain d1isvb2: 1isv B:501-803 [66344]
   Other proteins in same PDB: d1isva1, d1isvb1
   complexed with xys

Details for d1isvb2

PDB Entry: 1isv, 2.1 Å

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

SCOP Domain Sequences for d1isvb2:

Sequence; same for both SEQRES and ATOM records:

>d1isvb2 c.1.8.3 (B:501-803) Xylanase A, catalytic core {Streptomyces olivaceoviridis}
aestlgaaaaqsgryfgtaiasgklgdsayttiasrefnmvtaenemkidatepqrgqfn
fsagdrvynwavqngkqvrghtlawhsqqpgwmqslsgstlrqamidhingvmghykgki
aqwdvvneafsddgsggrrdsnlqrtgndwievafrtaraadpaaklcyndynienwtwa
ktqgvynmvrdfkqrgvpidcvgfqshfnsgspynsnfrttlqnfaalgvdvaiteldiq
gassstyaavtndclavsrclgitvwgvrdtdswrsgdtpllfngdgskkaaytavlnal
ngg

Timeline for d1isvb2:

• d1isvb2 first appeared in SCOP 1.59
  
• d1isvb2 appears in SCOP 1.63
  
• d1isvb2 appears in SCOP 1.67
  
• d1isvb2 appears in the current release, SCOPe 2.08