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PDBsum entry 4duv

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protein ligands metals Protein-protein interface(s) links
Hydrolase PDB id
4duv

 

 

 

 

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Contents
Protein chains
1019 a.a.
Ligands
2DG ×4
BTB ×4
DMS ×90
Metals
_MG ×9
_NA ×16
Waters ×4018
PDB id:
4duv
Name: Hydrolase
Title: E. Coli (lacz) beta-galactosidase (g974a) 2-deoxy-galactosyl-enzyme and bis-tris complex
Structure: Beta-galactosidase. Chain: a, b, c, d. Fragment: unp residues 10-1024. Synonym: beta-gal, lactase. Engineered: yes. Mutation: yes
Source: Escherichia coli. Organism_taxid: 83333. Strain: k12. Gene: b0344, jw0335, lacz. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
2.10Å     R-factor:   0.159     R-free:   0.206
Authors: R.W.Wheatley,S.Lo,L.J.Janzcewicz,M.L.Dugdale,R.E.Huber
Key ref: R.W.Wheatley et al. The glucose acceptor site of lacz beta-Galactosidase synthesis of allolactose - The natural inducer of the operon. To be published, .
Date:
22-Feb-12     Release date:   03-Apr-13    
PROCHECK
Go to PROCHECK summary
 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.
1019 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 5 residue positions (black crosses)

 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.

 

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