› 1lmt

X-ray diffraction
1.6Å resolution

STRUCTURE OF A CONFORMATIONALLY CONSTRAINED ARG-GLY-ASP SEQUENCE INSERTED INTO HUMAN LYSOZYME

Released:
DOI: 10.2210/pdb1lmt/pdb
PDB entry 1lmt coloured by chain, front view.
PDB entry 1lmt coloured by chain, side view.
PDB entry 1lmt coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structure of a conformationally constrained Arg-Gly-Asp sequence inserted into human lysozyme.
Yamada T, Song H, Inaka K, Shimada Y, Kikuchi M, Matsushima M
J Biol Chem 270 5687-90 (1995)
PMID: 7890692

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:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-158303 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Lysozyme C Chain: A
Molecule details ›
Chain: A
Length: 136 amino acids
Theoretical weight: 15.34 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P61626 (Residues: 19-92, 93-148; Coverage: 100%)
Gene names: LYZ, LZM
Sequence domains: C-type lysozyme/alpha-lactalbumin family
Structure domains: Lysozyme

Ligands and Environments

Carbohydrate polymer : NEW Components: NAG
Carbohydrate polymer
1 bound ligand:
Ligand CL 2 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P212121
Unit cell:
a: 56.49Å b: 61.46Å c: 33.42Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.176 0.176 not available
Expression system: Not provided

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Citations

1 review citation

Engineering novel proteins by transfer of active sites to natural scaffolds.
Vita C. (1997)
9 other articles