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protein Protein-protein interface(s) links
Hydrolase PDB id
1zcf
Jmol
Contents
Protein chains
(+ 2 more) 325 a.a. *
* Residue conservation analysis
PDB id:
1zcf
Name: Hydrolase
Title: L-asparaginase from erwinia carotovora
Structure: L-asparaginase. Chain: a, b, c, d, e, f, g, h. Engineered: yes
Source: Pectobacterium atrosepticum. Organism_taxid: 218491. Strain: scri1043. Gene: lans. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.
Biol. unit: Tetramer (from PQS)
Resolution:
3.00Å     R-factor:   0.203     R-free:   0.282
Authors: I.P.Kuranova,Y.A.Kislizin,O.V.Kravchenko,S.V.Nikonov
Key ref: Y.A.Kislizin et al. (2006). The crystal structure of l-Asparaginase from erwinia carotovora. Kristallografiya, 51, PubMed id: -1
Date:
12-Apr-05     Release date:   18-Apr-06    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
Q6Q4F4  (Q6Q4F4_ERWCT) -  L-asparaginase (Precursor)
Seq:
Struc:
346 a.a.
325 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 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
+ NH(3)
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     cellular amino acid metabolic process   2 terms 
  Biochemical function     asparaginase activity     1 term