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PDBsum entry 3ujs

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protein ligands metals Protein-protein interface(s) links
Lyase PDB id
3ujs

 

 

 

 

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JSmol PyMol  
Contents
Protein chains
433 a.a.
Ligands
XSP
TRS
0V5
Metals
_MG ×4
Waters ×806
PDB id:
3ujs
Name: Lyase
Title: Asymmetric complex of human neuron specific enolase-6-pga/pep
Structure: Gamma-enolase. Chain: a, b. Synonym: 2-phospho-d-glycerate hydro-lyase, enolase 2, neural enolase, neuron-specific enolase, nse. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: eno2. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
1.65Å     R-factor:   0.138     R-free:   0.185
Authors: J.Qin,G.Chai,J.Brewer,L.Lovelace,L.Lebioda
Key ref: J.Qin et al. (2012). Structures of asymmetric complexes of human neuron specific enolase with resolved substrate and product and an analogous complex with two inhibitors indicate subunit interaction and inhibitor cooperativity. J Inorg Biochem, 111, 187-194. PubMed id: 22437160
Date:
08-Nov-11     Release date:   22-Aug-12    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
P09104  (ENOG_HUMAN) -  Gamma-enolase from Homo sapiens
Seq:
Struc:
434 a.a.
433 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.4.2.1.11  - phosphopyruvate hydratase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: (2R)-2-phosphoglycerate = phosphoenolpyruvate + H2O
(2R)-2-phosphoglycerate
= phosphoenolpyruvate
+ H2O
Bound ligand (Het Group name = XSP)
matches with 90.91% similarity
      Cofactor: Mg(2+)
Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 

 
    Key reference    
 
 
J Inorg Biochem 111:187-194 (2012)
PubMed id: 22437160  
 
 
Structures of asymmetric complexes of human neuron specific enolase with resolved substrate and product and an analogous complex with two inhibitors indicate subunit interaction and inhibitor cooperativity.
J.Qin, G.Chai, J.M.Brewer, L.L.Lovelace, L.Lebioda.
 
  ABSTRACT  
 
No abstract given.

 

 

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