8dmk

Electron Microscopy
3.7Å resolution

Cryo-EM reveals the molecular basis of laminin polymerization and LN-lamininopathies

Released:
Source organism: Homo sapiens
Related structures: EMD-27542

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
PDBe Complex ID:
PDB-CPX-226725 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Laminin subunit alpha-1 Chain: A
Molecule details ›
Chain: A
Length: 305 amino acids
Theoretical weight: 34.71 KDa
Source organism: Homo sapiens
Expression system: Homo sapiens
UniProt:
  • Canonical: P19137 (Residues: 28-332; Coverage: 10%)
Gene names: Lama, Lama-1, Lama1
Sequence domains:
Laminin subunit beta-1 Chain: B
Molecule details ›
Chain: B
Length: 307 amino acids
Theoretical weight: 35.09 KDa
Source organism: Homo sapiens
Expression system: Homo sapiens
UniProt:
  • Canonical: P07942 (Residues: 29-335; Coverage: 17%)
Gene name: LAMB1
Sequence domains:
Laminin subunit gamma-1 Chain: G
Molecule details ›
Chain: G
Length: 305 amino acids
Theoretical weight: 34.11 KDa
Source organism: Homo sapiens
Expression system: Homo sapiens
UniProt:
  • Canonical: P11047 (Residues: 37-341; Coverage: 19%)
Gene names: LAMB2, LAMC1
Sequence domains:

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
Resolution: 3.7Å
Relevant EMDB volumes: EMD-27542
Expression system: Homo sapiens