› 3t2p

X-ray diffraction
2.6Å resolution

E. coli (lacZ) beta-galactosidase (S796D) in complex with IPTG

Released:
DOI: 10.2210/pdb3t2p/pdb
PDB entry 3t2p coloured by chain, front view.
PDB entry 3t2p coloured by chain, side view.
PDB entry 3t2p coloured by chain, top view.
Source organism: Escherichia coli K-12
Primary publication:
Ser-796 of β-galactosidase (Escherichia coli) plays a key role in maintaining a balance between the opened and closed conformations of the catalytically important active site loop.
Jancewicz LJ, Wheatley RW, Sutendra G, Lee M, Fraser ME, Huber RE
Arch Biochem Biophys 517 111-22 (2012)
PMID: 22155115

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: 119.77 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

4 bound ligands:
Ligand IPT 4 x IPT
Ligand MG 8 x MG
Ligand NA 10 x NA
Ligand DMS 63 x DMS
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.3.1
Spacegroup: P212121
Unit cell:
a: 150.869Å b: 166.171Å c: 200.786Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.185 0.184 0.242
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