› 3muz

X-ray diffraction
1.9Å resolution

E.Coli (lacZ) beta-galactosidase (R599A) in complex with IPTG

Released:
DOI: 10.2210/pdb3muz/pdb
PDB entry 3muz coloured by chain, front view.
PDB entry 3muz coloured by chain, side view.
PDB entry 3muz coloured by chain, top view.
Source organism: Escherichia coli K-12
Primary publication:
Importance of Arg-599 of b-galactosidase (Escherichia coli) as an anchor for the open conformations of Phe-601 and the active-site loop
Dugdale ML, Vance ML, Wheatley RW, Driedger MR, Nibber A, Tran A, Huber RE
Biochem. Cell Biol. 88 969-979 (2010)

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: 1, 2, 3, 4
Molecule details ›
Chains: 1, 2, 3, 4
Length: 1052 amino acids
Theoretical weight: 119.66 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 8 x IPT
Ligand MG 14 x MG
Ligand NA 16 x NA
Ligand DMS 150 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: 151.83Å b: 163.28Å c: 204.2Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.219 0.219 0.248
Expression system: Escherichia coli

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