SCOPe 2.02: Domain d1v6va2: 1v6v A:1-303

Lineage for d1v6va2 (1v6v A:1-303)

1. Root: SCOPe 2.02

2. Class c: Alpha and beta proteins (a/b) [51349] (147 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 d1v6va2: 1v6v A:1-303 [100431]
   Other proteins in same PDB: d1v6va1, d1v6vb1
   complexed with xyp

Details for d1v6va2

PDB Entry: 1v6v, 2.1 Å

PDB Description: crystal structure of xylanase from streptomyces olivaceoviridis e-86 complexed with 3(2)-alpha-l-arabinofuranosyl-xylotriose

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

SCOPe Domain Sequences for d1v6va2:

Sequence; same for both SEQRES and ATOM records:

>d1v6va2 c.1.8.3 (A:1-303) Xylanase A, catalytic core {Streptomyces olivaceoviridis [TaxId: 1921]}
aestlgaaaaqsgryfgtaiasgklgdsayttiasrefnmvtaenemkidatepqrgqfn
fsagdrvynwavqngkqvrghtlawhsqqpgwmqslsgstlrqamidhingvmghykgki
aqwdvvneafsddgsggrrdsnlqrtgndwievafrtaraadpaaklcyndynienwtwa
ktqgvynmvrdfkqrgvpidcvgfqshfnsgspynsnfrttlqnfaalgvdvaiteldiq
gassstyaavtndclavsrclgitvwgvrdtdswrsgdtpllfngdgskkaaytavlnal
ngg

Timeline for d1v6va2:

• d1v6va2 first appeared in SCOP 1.67
  
• d1v6va2 appears in SCOPe 2.01
  
• d1v6va2 appears in SCOPe 2.03
  
• d1v6va2 appears in the current release, SCOPe 2.08