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PDBsum entry 3vdb

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

 

 

 

 

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Contents
Protein chains
1015 a.a.
Ligands
149 ×4
DMS ×77
Metals
_MG ×9
_NA ×14
Waters ×3458
PDB id:
3vdb
Name: Hydrolase
Title: E. Coli (lacz) beta-galactosidase (n460t) in complex with galactonolactone
Structure: Beta-galactosidase. Chain: a, b, c, d. Synonym: beta-gal, lactase. Engineered: yes. Mutation: yes
Source: Escherichia coli. Organism_taxid: 562. Gene: lacz. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
2.05Å     R-factor:   0.157     R-free:   0.205
Authors: R.W.Wheatley,J.C.Kappelhoff,J.N.Hahn,M.L.Dugdale,M.J.Dutkoski, S.D.Tamman,M.E.Fraser,R.E.Huber
Key ref: R.W.Wheatley et al. (2012). Substitution for Asn460 cripples β-galactosidase (Escherichia coli) by increasing substrate affinity and decreasing transition state stability. Arch Biochem Biophys, 521, 51-61. PubMed id: 22446164
Date:
04-Jan-12     Release date:   11-Apr-12    
PROCHECK
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 Headers
 References

Protein chains
Pfam   ArchSchema ?
P00722  (BGAL_ECOLI) -  Beta-galactosidase from Escherichia coli (strain K12)
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
1024 a.a.
1015 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 1 residue position (black cross)

 Enzyme reactions 
   Enzyme class: E.C.3.2.1.23  - beta-galactosidase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Hydrolysis of terminal, non-reducing beta-D-galactose residues in beta-D-galactosides.

 

 
Arch Biochem Biophys 521:51-61 (2012)
PubMed id: 22446164  
 
 
Substitution for Asn460 cripples β-galactosidase (Escherichia coli) by increasing substrate affinity and decreasing transition state stability.
R.W.Wheatley, J.C.Kappelhoff, J.N.Hahn, M.L.Dugdale, M.J.Dutkoski, S.D.Tamman, M.E.Fraser, R.E.Huber.
 
  ABSTRACT  
 
No abstract given.

 

 

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