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protein ligands metals Protein-protein interface(s) links
Hydrolase PDB id
1yi7
Jmol
Contents
Protein chains
534 a.a. *
Ligands
SO4 ×7
EPE ×4
GOL ×20
Metals
_CA ×4
Waters ×2586
* Residue conservation analysis
PDB id:
1yi7
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 PQS)
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
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
Q97DM1  (Q97DM1_CLOAB) -  Beta-xylosidase, family 43 glycosyl hydrolase
Seq:
Struc:
 
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 
  GO annot!
  Biological process     carbohydrate metabolic process   1 term 
  Biochemical function     hydrolase activity     3 terms