› 1f4a

X-ray diffraction
2.8Å resolution

E. COLI (LACZ) BETA-GALACTOSIDASE (NCS CONSTRAINED MONOMER-ORTHORHOMBIC)

Released:
DOI: 10.2210/pdb1f4a/pdb
PDB entry 1f4a coloured by chain, front view.
PDB entry 1f4a coloured by chain, side view.
PDB entry 1f4a coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
High resolution refinement of beta-galactosidase in a new crystal form reveals multiple metal-binding sites and provides a structural basis for alpha-complementation.
Juers DH, Jacobson RH, Wigley D, Zhang XJ, Huber RE, Tronrud DE, Matthews BW
Protein Sci 9 1685-99 (2000)
PMID: 11045615

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 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: 1021 amino acids
Theoretical weight: 116.24 KDa
Source organism: Escherichia coli
UniProt:
  • Canonical: P00722 (Residues: 4-1024; Coverage: 100%)
Gene names: JW0335, b0344, lacZ
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand MG 8 x MG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SRS
Spacegroup: P212121
Unit cell:
a: 153.4Å b: 173.4Å c: 204.4Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.167 0.167 0.198

Quick links

Citations

15 review citations

Role of Na+ and K+ in enzyme function.
Page et al. (2006)
14 more

3 mentions without citation

An integrated native mass spectrometry and top-down proteomics method that connects sequence to structure and function of macromolecular complexes.
Li et al. (2018)
2 more