› 224l

X-ray diffraction
1.85Å resolution

THE ENERGETIC COST AND THE STRUCTURAL CONSEQUENCES OF BURYING A HYDROXYL GROUP WITHIN THE CORE OF A PROTEIN DETERMINED FROM ALA TO SER AND VAL TO THR SUBSTITUTIONS IN T4 LYSOZYME

Released:
DOI: 10.2210/pdb224l/pdb
PDB entry 224l coloured by chain, front view.
PDB entry 224l coloured by chain, side view.
PDB entry 224l coloured by chain, top view.
Source organism: Escherichia virus T4
Primary publication:
Energetic cost and structural consequences of burying a hydroxyl group within the core of a protein determined from Ala-->Ser and Val-->Thr substitutions in T4 lysozyme.
Blaber M, Lindstrom JD, Gassner N, Xu J, Heinz DW, Matthews BW
Biochemistry 32 11363-73 (1993)
PMID: 8218201

Function and Biology Details

Reaction catalysed: 
Hydrolysis of (1->4)-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in a peptidoglycan and between N-acetyl-D-glucosamine residues in chitodextrins
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-133020 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Endolysin Chain: A
Molecule details ›
Chain: A
Length: 164 amino acids
Theoretical weight: 18.64 KDa
Source organism: Escherichia virus T4
Expression system: Not provided
UniProt:
  • Canonical: P00720 (Residues: 1-164; Coverage: 100%)
Gene name: E
Sequence domains: Phage lysozyme
Structure domains: Lysozyme

Ligands and Environments

2 bound ligands:
Ligand CL 2 x CL
Ligand BME 1 x BME
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P3221
Unit cell:
a: 61.1Å b: 61.1Å c: 97Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.164 not available not available
Expression system: Not provided

Quick links

Citations

4 review citations

Energetics of protein folding.
Baldwin RL. (2007)
3 more

4 mentions without citation

Common origin of four diverse families of large eukaryotic DNA viruses.
Iyer et al. (2001)
3 more