› 2y38

X-ray diffraction
2.9Å resolution

LAMININ ALPHA5 CHAIN N-TERMINAL FRAGMENT

Released:
DOI: 10.2210/pdb2y38/pdb
PDB entry 2y38 coloured by chain, front view.
PDB entry 2y38 coloured by chain, side view.
PDB entry 2y38 coloured by chain, top view.
Source organism: Mus musculus
Primary publication:
Determinants of laminin polymerization revealed by the structure of the α5 chain amino-terminal region.
Hussain SA, Carafoli F, Hohenester E
EMBO Rep 12 276-82 (2011)
PMID: 21311558

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-178850 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Laminin subunit alpha-5 Chain: A
Molecule details ›
Chain: A
Length: 403 amino acids
Theoretical weight: 44.76 KDa
Source organism: Mus musculus
Expression system: Homo sapiens
UniProt:
  • Canonical: Q61001 (Residues: 44-433; Coverage: 11%)
Gene name: Lama5
Sequence domains:
Structure domains:

Ligands and Environments

Carbohydrate polymer : NEW Components: NAG
Carbohydrate polymer
2 bound ligands:
Ligand NAG 1 x NAG
Ligand PO4 6 x PO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I02
Spacegroup: P62
Unit cell:
a: 116.4Å b: 116.4Å c: 112.3Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.254 0.254 0.292
Expression system: Homo sapiens

Quick links

Citations

13 review citations

Laminins in basement membrane assembly.
Hohenester et al. (2013)
12 more

7 mentions without citation

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