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PDBsum entry 2f6b

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protein Protein-protein interface(s) links
Hydrolase PDB id
2f6b
Jmol
Contents
Protein chains
206 a.a. *
Waters ×45
* Residue conservation analysis
PDB id:
2f6b
Name: Hydrolase
Title: Structural and active site modification studies implicate glu, trp and arg in the activity of xylanase from alkalophilic bacillus sp. (Ncl 87-6-10).
Structure: Family 11 xylanase. Chain: a, b. Ec: 3.2.1.8
Source: Bacillus. Organism_taxid: 1386. Other_details: soil
Biol. unit: Dimer (from PQS)
Resolution:
2.80Å     R-factor:   0.169     R-free:   0.226
Authors: L.Satyanarayana,H.Balakrishnan,S.Gaikward,C.G.Suresh
Key ref: H.Balakrishnan et al. Structural and active site modification studies implicate glu, Trp and arg in the activity of xylanase from alkalophilic bacillus sp. (Ncl 87-6-10).. To be published, .
Date:
29-Nov-05     Release date:   13-Dec-05    
PROCHECK
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 Headers
 References

Protein chains
Pfam   ArchSchema ?
Q7SIE3  (Q7SIE3_BACAG) -  Endo-1,4-beta-xylanase
Seq:
Struc:
207 a.a.
206 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 4 residue positions (black crosses)

 Enzyme reactions 
   Enzyme class: E.C.3.2.1.8  - Endo-1,4-beta-xylanase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Endohydrolysis of 1,4-beta-D-xylosidic linkages in xylans.
 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     metabolic process   3 terms 
  Biochemical function     hydrolase activity     4 terms