 |
|
|
|
|
 |
Contents |
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
* Residue conservation analysis
|
|
|
|
|
PDB id:
|
 |
|
 |
| Name: |
 |
Hydrolase
|
 |
|
Title:
|
 |
Beta-d-xylosidase (selenomethionine) xynd from clostridium acetobutylicum
|
|
Structure:
|
 |
Beta-xylosidase, family 43 glycosyl hydrolase. Chain: a, b, c, d. Engineered: yes
|
|
Source:
|
 |
Clostridium acetobutylicum. Organism_taxid: 272562. Strain: atcc 824. Gene: cac3452 (xynd). Expressed in: escherichia coli bl21. Expression_system_taxid: 511693.
|
|
Biol. unit:
|
 |
Dimer (from
)
|
|
Resolution:
|
 |
|
1.90Å
|
R-factor:
|
0.144
|
R-free:
|
0.202
|
|
|
Authors:
|
 |
A.Teplyakov,E.Fedorov,G.L.Gilliland,S.C.Almo,S.K.Burley,New Research Center For Structural Genomics (Nysgxrc)
|
|
Key ref:
|
 |
A.Teplyakov
et al.
Crystal structure of beta-Xylosidase from clostridium acetobutylicum.
To be published,
|
 |
|
Date:
|
 |
|
11-Jan-05
|
Release date:
|
22-Feb-05
|
|
|
|
|
|
PROCHECK
|
|
|
|
|
Headers
|
 |
|
|
References
|
|
|
|
|
|
|
Q97DM1
(Q97DM1_CLOAB) -
Beta-xylosidase, family 43 glycosyl hydrolase
|
|
|
|
Seq: Struc:
|
 |
 |
 |
533 a.a.
534 a.a.*
|
|
|
|
|
|
|
 |
 |
|
|
Key: |
 |
PfamA domain |
 |
 |
 |
Secondary structure |
 |
 |
CATH domain |
 |
|
*
PDB and UniProt seqs differ
at 2 residue positions (black
crosses)
|
|
|
|
|
 |
|
 |
|
 |
|
|
Gene Ontology (GO) functional annotation
|
|
|
|
 |
 |
 |
|
 |
 |
 |
 |
|
 |
|
Biological process
|
carbohydrate metabolic process
|
1 term
|
 |
|
Biochemical function
|
hydrolase activity
|
3 terms
|
 |
|
|
 |
 |
 |
 |
 |
 |
|