› 1q7d

X-ray diffraction
1.8Å resolution

Structure of the integrin alpha2beta1 binding collagen peptide

Released:
DOI: 10.2210/pdb1q7d/pdb
PDB entry 1q7d coloured by chain, front view.
PDB entry 1q7d coloured by chain, side view.
PDB entry 1q7d coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structure of the integrin alpha2beta1-binding collagen peptide.
Emsley J, Knight CG, Farndale RW, Barnes MJ
J Mol Biol 335 1019-28 (2004)
PMID: 14698296

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-135851 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Collagen alpha-1(I) chain Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 23 amino acids
Theoretical weight: 2.04 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P02452 (Residues: 133-153; Coverage: 2%)
Gene name: COL1A1
Sequence domains: Collagen triple helix repeat (20 copies)

Ligands and Environments

No bound ligands
1 modified residue:
Ligand HYP 18 x HYP

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID13
Spacegroup: C2221
Unit cell:
a: 29.6Å b: 135.8Å c: 25.4Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.236 0.236 0.266
Expression system: Not provided

Quick links

Citations

12 review citations

Nanoscale engineering of biomimetic surfaces: cues from the extracellular matrix.
von der Mark et al. (2010)
11 more

8 mentions without citation

Aromatic interactions promote self-association of collagen triple-helical peptides to higher-order structures.
Kar et al. (2009)
7 more