› 3dyp

X-ray diffraction
1.75Å resolution

E. coli (lacZ) beta-galactosidase (H418N)

Released:
DOI: 10.2210/pdb3dyp/pdb
PDB entry 3dyp coloured by chain, front view.
PDB entry 3dyp coloured by chain, side view.
PDB entry 3dyp coloured by chain, top view.
Source organism: Escherichia coli K-12
Primary publication:
Direct and indirect roles of His-418 in metal binding and in the activity of beta-galactosidase (E. coli).
Juers DH, Rob B, Dugdale ML, Rahimzadeh N, Giang C, Lee M, Matthews BW, Huber RE
Protein Sci 18 1281-92 (2009)
PMID: 19472413

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: 1023 amino acids
Theoretical weight: 116.48 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli
UniProt:
  • Canonical: P00722 (Residues: 10-1024; Coverage: 99%)
Gene names: JW0335, b0344, lacZ
Sequence domains:
Structure domains:

Ligands and Environments

3 bound ligands:
Ligand MG 16 x MG
Ligand NA 16 x NA
Ligand DMS 107 x DMS
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL7-1
Spacegroup: P212121
Unit cell:
a: 149.38Å b: 168.02Å c: 200.29Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.159 0.159 0.217
Expression system: Escherichia coli

Quick links

Citations

2 review citations

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

2 mentions without citation

Direct and indirect roles of His-418 in metal binding and in the activity of beta-galactosidase (E. coli).
Juers et al. (2009)
1 more