› 104l

X-ray diffraction
2.8Å resolution

HOW AMINO-ACID INSERTIONS ARE ALLOWED IN AN ALPHA-HELIX OF T4 LYSOZYME

Released:
DOI: 10.2210/pdb104l/pdb
PDB entry 104l coloured by chain, front view.
PDB entry 104l coloured by chain, side view.
PDB entry 104l coloured by chain, top view.
Source organism: Tequatrovirus T4
Primary publication:
How amino-acid insertions are allowed in an alpha-helix of T4 lysozyme.
Heinz DW, Baase WA, Dahlquist FW, Matthews BW
Nature 361 561-4 (1993)
PMID: 8429913

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:
  • not assigned
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 Chains: A, B
Molecule details ›
Chains: A, B
Length: 166 amino acids
Theoretical weight: 18.77 KDa
Source organism: Tequatrovirus T4
Expression system: Not provided
UniProt:
  • Canonical: P00720 (Residues: 1-44, 45-164; Coverage: 100%)
Gene name: E
Sequence domains: Phage lysozyme
Structure domains: Lysozyme

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: R32
Unit cell:
a: 172.1Å b: 172.1Å c: 80Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.175 not available not available
Expression system: Not provided

Quick links

Citations

12 review citations

Helical membrane protein folding, stability, and evolution.
Popot et al. (2000)
11 more

9 mentions without citation

Flaviviral NS4b, chameleon and jack-in-the-box roles in viral replication and pathogenesis, and a molecular target for antiviral intervention.
Zmurko et al. (2015)
8 more