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PDBsum entry 2wnn

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protein ligands metals Protein-protein interface(s) links
Lyase PDB id
2wnn

 

 

 

 

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Contents
Protein chains
296 a.a. *
Ligands
1PE ×3
Metals
_NA
Waters ×758
* Residue conservation analysis
PDB id:
2wnn
Name: Lyase
Title: Structure of wild type e. Coli n-acetylneuraminic acid lyase in complex with pyruvate in space group p21
Structure: N-acetylneuraminate lyase. Chain: a, b, c, d. Fragment: residues 2-296. Synonym: n-acetylneuraminic acid lyase, n-acetylneuraminate pyruvate- lyase, sialic acid lyase, sialate lyase, sialic acid aldolase, nalase. Engineered: yes. Other_details: schiff base between lys165 and pyruvate in all chains
Source: Escherichia coli. Organism_taxid: 562. Expressed in: escherichia coli. Expression_system_taxid: 469008.
Resolution:
1.65Å     R-factor:   0.212     R-free:   0.249
Authors: I.Campeotto,A.H.Bolt,T.A.Harman,C.H.Trinh,C.A.Dennis,S.E.V.Phillips, A.R.Pearson,A.Nelson,A.Berry
Key ref: I.Campeotto et al. (2010). Structural insights into substrate specificity in variants of N-acetylneuraminic Acid lyase produced by directed evolution. J Mol Biol, 404, 56-69. PubMed id: 20826162
Date:
13-Jul-09     Release date:   25-Aug-10    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
P0A6L4  (NANA_ECOLI) -  N-acetylneuraminate lyase from Escherichia coli (strain K12)
Seq:
Struc:
297 a.a.
296 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 2 residue positions (black crosses)

 Enzyme reactions 
   Enzyme class: E.C.4.1.3.3  - N-acetylneuraminate lyase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: aceneuramate = aldehydo-N-acetyl-D-mannosamine + pyruvate
aceneuramate
= aldehydo-N-acetyl-D-mannosamine
+
pyruvate
Bound ligand (Het Group name = 1PE)
matches with 44.44% similarity
Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 

 
    Key reference    
 
 
J Mol Biol 404:56-69 (2010)
PubMed id: 20826162  
 
 
Structural insights into substrate specificity in variants of N-acetylneuraminic Acid lyase produced by directed evolution.
I.Campeotto, A.H.Bolt, T.A.Harman, C.Dennis, C.H.Trinh, S.E.Phillips, A.Nelson, A.R.Pearson, A.Berry.
 
  ABSTRACT  
 
No abstract given.

 

 

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