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PDBsum entry 3ljq

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protein ligands metals Protein-protein interface(s) links
Hydrolase PDB id
3ljq

 

 

 

 

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Contents
Protein chains
281 a.a. *
Ligands
GLY
Metals
_NA ×2
Waters ×512
* Residue conservation analysis
PDB id:
3ljq
Name: Hydrolase
Title: Crystal structure of the glycosylasparaginase t152c apo-precursor
Structure: N(4)-(beta-n-acetylglucosaminyl)-l-asparaginase. Chain: a, c. Fragment: unp residues 46-340. Synonym: glycosylasparaginase, aspartylglucosaminidase, aga, n4-(n- acetyl-beta-glucosaminyl)-l-asparagine amidase, glycosylasparaginase alpha chain, glycosylasparaginase beta chain. Engineered: yes. Mutation: yes
Source: Flavobacterium meningosepticum. Organism_taxid: 238. Gene: ga(1-295). Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
1.90Å     R-factor:   0.154     R-free:   0.197
Authors: Y.Wang,H.-C.Guo
Key ref: Y.Wang and H.C.Guo (2010). Crystallographic snapshot of glycosylasparaginase precursor poised for autoprocessing. J Mol Biol, 403, 120-130. PubMed id: 20800597
Date:
26-Jan-10     Release date:   24-Nov-10    
PROCHECK
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 Headers
 References

Protein chains
Pfam   ArchSchema ?
Q47898  (ASPG_ELIMR) -  N(4)-(Beta-N-acetylglucosaminyl)-L-asparaginase from Elizabethkingia miricola
Seq:
Struc:
340 a.a.
281 a.a.*
Key:    PfamA domain  Secondary structure
* PDB and UniProt seqs differ at 1 residue position (black cross)

 Enzyme reactions 
   Enzyme class: E.C.3.5.1.26  - N(4)-(beta-N-acetylglucosaminyl)-L-asparaginase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: N4-(beta-N-acetyl-D-glucosaminyl)-L-asparagine + H2O = N-acetyl-beta-D- glucosaminylamine + L-aspartate + H+
N(4)-(beta-N-acetyl-D-glucosaminyl)-L-asparagine
+ H2O
= N-acetyl-beta-D- glucosaminylamine
+
L-aspartate
Bound ligand (Het Group name = GLY)
matches with 55.56% similarity
+ H(+)
Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 

 
    Added reference    
 
 
J Mol Biol 403:120-130 (2010)
PubMed id: 20800597  
 
 
Crystallographic snapshot of glycosylasparaginase precursor poised for autoprocessing.
Y.Wang, H.C.Guo.
 
  ABSTRACT  
 
No abstract given.

 

 

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