› 1klo

X-ray diffraction
2.1Å resolution

CRYSTAL STRUCTURE OF THREE CONSECUTIVE LAMININ-TYPE EPIDERMAL GROWTH FACTOR-LIKE (LE) MODULES OF LAMININ GAMMA1 CHAIN HARBORING THE NIDOGEN BINDING SITE

Released:
DOI: 10.2210/pdb1klo/pdb
PDB entry 1klo coloured by chain, front view.
PDB entry 1klo coloured by chain, side view.
PDB entry 1klo coloured by chain, top view.
Source organism: Mus musculus
Primary publication:
Crystal structure of three consecutive laminin-type epidermal growth factor-like (LE) modules of laminin gamma1 chain harboring the nidogen binding site.
Stetefeld J, Mayer U, Timpl R, Huber R
J Mol Biol 257 644-57 (1996)
PMID: 8648630

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domain:
Structure domain:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-135869 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Laminin subunit gamma-1 Chain: A
Molecule details ›
Chain: A
Length: 162 amino acids
Theoretical weight: 17.14 KDa
Source organism: Mus musculus
UniProt:
  • Canonical: P02468 (Residues: 771-932; Coverage: 10%)
Gene names: Lamb-2, Lamc-1, Lamc1
Sequence domains: Laminin EGF domain
Structure domains: Laminin

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P6422
Unit cell:
a: 74.57Å b: 74.57Å c: 185.11Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.197 0.197 not available

Quick links

Citations

20 review citations

Protein tyrosine kinase structure and function.
Hubbard et al. (2000)
19 more

8 mentions without citation

Structural biology of laminins.
Hohenester E. (2019)
7 more