› 3vd7

X-ray diffraction
2.87Å resolution

E. coli (lacZ) beta-galactosidase (N460S) in complex with galactotetrazole

Released:
DOI: 10.2210/pdb3vd7/pdb
PDB entry 3vd7 coloured by chain, front view.
PDB entry 3vd7 coloured by chain, side view.
PDB entry 3vd7 coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Substitution for Asn460 cripples β-galactosidase (Escherichia coli) by increasing substrate affinity and decreasing transition state stability.
Wheatley RW, Kappelhoff JC, Hahn JN, Dugdale ML, Dutkoski MJ, Tamman SD, Fraser ME, Huber RE
Arch Biochem Biophys 521 51-61 (2012)
PMID: 22446164

Function and Biology Details

Reaction catalysed: 
Hydrolysis of terminal non-reducing beta-D-galactose residues in beta-D-galactosides
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-133036 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Beta-galactosidase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 1052 amino acids
Theoretical weight: 119.72 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P00722 (Residues: 10-1024; Coverage: 99%)
Gene names: JW0335, b0344, lacZ
Sequence domains:
Structure domains:

Ligands and Environments

4 bound ligands:
Ligand GTZ 4 x GTZ
Ligand MG 6 x MG
Ligand NA 8 x NA
Ligand DMS 29 x DMS
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.3.1
Spacegroup: P21
Unit cell:
a: 128.46Å b: 152.37Å c: 135.11Å
α: 90° β: 104.25° γ: 90°
R-values:
R R work R free
0.19 0.188 0.25
Expression system: Escherichia coli

Quick links

Citations

1 review citation

LacZ β-galactosidase: structure and function of an enzyme of historical and molecular biological importance.
Juers et al. (2012)
8 other articles

1 mention without citation

Intrinsic dynamic behavior of enzyme:substrate complexes govern the catalytic action of β-galactosidases across clan GH-A.
Kumar et al. (2019)