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Hydrolase PDB id
2wt4
Jmol
Contents
Protein chain
315 a.a. *
Ligands
ASP
Waters ×168
* Residue conservation analysis
PDB id:
2wt4
Name: Hydrolase
Title: Room temperature crystal structure of helicobacter pylori l- asparaginase at 1.8 a resolution
Structure: L-asparaginase. Chain: a. Synonym: l-asnase. Engineered: yes
Source: Helicobacter pylori. Organism_taxid: 210. Expressed in: escherichia coli. Expression_system_taxid: 562
Resolution:
1.80Å     R-factor:   0.153     R-free:   0.184
Authors: P.Dhavala,A.C.Papageorgiou
Key ref: P.Dhavala and a.c.papageorgiou (2009). Structure of helicobacter pylori l-Asparaginase at 1.4 a resolution. Acta crystallogr.,Sect.D, 65,
Date:
11-Sep-09     Release date:   24-Nov-09    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
Q9ZLB9  (ASPG_HELPJ) -  Probable L-asparaginase
Seq:
Struc:
332 a.a.
315 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 3 residue positions (black crosses)

 Enzyme reactions 
   Enzyme class: E.C.3.5.1.1  - Asparaginase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: L-asparagine + H2O = L-aspartate + NH3
L-asparagine
+ H(2)O
=
L-aspartate
Bound ligand (Het Group name = ASP)
corresponds exactly
+ NH(3)
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     cytoplasm   1 term 
  Biological process     cellular amino acid metabolic process   2 terms 
  Biochemical function     hydrolase activity     2 terms