› 148l

X-ray diffraction
1.9Å resolution

A COVALENT ENZYME-SUBSTRATE INTERMEDIATE WITH SACCHARIDE DISTORTION IN A MUTANT T4 LYSOZYME

Released:
DOI: 10.2210/pdb148l/pdb
PDB entry 148l coloured by chain, front view.
PDB entry 148l coloured by chain, side view.
PDB entry 148l coloured by chain, top view.
Source organisms:
Primary publication:
A covalent enzyme-substrate intermediate with saccharide distortion in a mutant T4 lysozyme.
Kuroki R, Weaver LH, Matthews BW
Science 262 2030-3 (1993)
PMID: 8266098

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:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-133026 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (3 distinct):
Endolysin Chain: E
Molecule details ›
Chain: E
Length: 164 amino acids
Theoretical weight: 18.66 KDa
Source organism: Tequatrovirus T4
Expression system: Not provided
UniProt:
  • Canonical: P00720 (Residues: 1-164; Coverage: 100%)
Gene name: E
Sequence domains: Phage lysozyme
Structure domains: Lysozyme
SUBSTRATE CLEAVED FROM CELL WALL OF ESCHERICHIA COLI Chain: S
Molecule details ›
Chain: S
Length: 4 amino acids
Theoretical weight: 461 Da
Source organism: Escherichia coli

Ligands and Environments

Carbohydrate polymer : NEW Components: MUB, NAG
Carbohydrate polymer
1 bound ligand:
Ligand BME 1 x BME
3 modified residues:
Ligand FGA 1 x FGA
Ligand API 1 x API
Ligand DAL 1 x DAL

Experiments and Validation Details

Entry percentile scores
Spacegroup: P21212
Unit cell:
a: 50.9Å b: 67.3Å c: 49.6Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.168 not available not available
Expression system: Not provided

Quick links

Citations

16 review citations

Structures and mechanisms of glycosyl hydrolases.
Davies et al. (1995)
15 more

17 mentions without citation

Improvement in protein functional site prediction by distinguishing structural and functional constraints on protein family evolution using computational design.
Cheng et al. (2005)
16 more