› 172l

X-ray diffraction
1.9Å resolution

PROTEIN FLEXIBILITY AND ADAPTABILITY SEEN IN 25 CRYSTAL FORMS OF T4 LYSOZYME

Released:
DOI: 10.2210/pdb172l/pdb
PDB entry 172l coloured by chain, front view.
PDB entry 172l coloured by chain, side view.
PDB entry 172l coloured by chain, top view.
Source organism: Escherichia virus T4
Primary publication:
Protein flexibility and adaptability seen in 25 crystal forms of T4 lysozyme.
Zhang XJ, Wozniak JA, Matthews BW
J Mol Biol 250 527-52 (1995)
PMID: 7616572

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: 18.65 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

1 bound ligand:
Ligand BME 1 x BME
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P212121
Unit cell:
a: 32.2Å b: 50.4Å c: 97.1Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.19 not available not available
Expression system: Not provided

Quick links

Citations

6 review citations

Binding of small-molecule ligands to proteins: "what you see" is not always "what you get".
Mobley et al. (2009)
5 more

7 mentions without citation

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