› 2g66

X-ray diffraction
1.8Å resolution

Crystal structure of a collagen-like peptide with 3(S)Hyp in the Xaa position

Released:
DOI: 10.2210/pdb2g66/pdb
PDB entry 2g66 coloured by chain, front view.
PDB entry 2g66 coloured by chain, side view.
PDB entry 2g66 coloured by chain, top view.
Source organism: Synthetic construct
Primary publication:
The crystal structure of a collagen-like polypeptide with 3(S)-hydroxyproline residues in the Xaa position forms a standard 7/2 collagen triple helix.
Schumacher MA, Mizuno K, Bächinger HP
J Biol Chem 281 27566-74 (2006)
PMID: 16798737

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-162709 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
collagen Chains: A, B, G
Molecule details ›
Chains: A, B, G
Length: 31 amino acids
Theoretical weight: 2.78 KDa
Source organism: Synthetic construct
Expression system: Not provided

Ligands and Environments

No bound ligands
2 modified residues:
Ligand HYP 30 x HYP
Ligand HY3 6 x HY3

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.2.1
Spacegroup: P21
Unit cell:
a: 18.12Å b: 19.45Å c: 81.5Å
α: 90° β: 91.26° γ: 90°
R-values:
R R work R free
0.275 0.272 0.292
Expression system: Not provided

Quick links

Citations

8 review citations

The importance of proline residues in the structure, stability and susceptibility to proteolytic degradation of collagens.
Krane SM. (2008)
7 more

1 mention without citation

Collagen structure and stability.
Shoulders et al. (2009)