› 2jd4

X-ray diffraction
1.9Å resolution

Mouse laminin alpha1 chain, domains LG4-5

Released:
DOI: 10.2210/pdb2jd4/pdb
PDB entry 2jd4 coloured by chain, front view.
PDB entry 2jd4 coloured by chain, side view.
PDB entry 2jd4 coloured by chain, top view.
Source organism: Mus musculus
Primary publication:
Crystal structure and cell surface anchorage sites of laminin alpha1LG4-5.
Harrison D, Hussain SA, Combs AC, Ervasti JM, Yurchenco PD, Hohenester E
J Biol Chem 282 11573-81 (2007)
PMID: 17307732

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-148509 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Laminin subunit alpha-1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 383 amino acids
Theoretical weight: 41.9 KDa
Source organism: Mus musculus
Expression system: Homo sapiens
UniProt:
  • Canonical: P19137 (Residues: 2703-3083; Coverage: 13%)
Gene names: Lama, Lama-1, Lama1
Sequence domains:
Structure domains: Jelly Rolls

Ligands and Environments

2 bound ligands:
Ligand MG 4 x MG
Ligand CL 3 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SRS BEAMLINE PX9.6
Spacegroup: P21
Unit cell:
a: 70.53Å b: 55.812Å c: 100.986Å
α: 90° β: 98.48° γ: 90°
R-values:
R R work R free
0.23 0.23 0.262
Expression system: Homo sapiens

Quick links

Citations

8 review citations

Basement membranes: cell scaffoldings and signaling platforms.
Yurchenco PD. (2011)
7 more

15 mentions without citation

Laminin 332 processing impacts cellular behavior.
Rousselle et al. (2013)
14 more