› 5k31

X-ray diffraction
2.2Å resolution

Crystal structure of Human fibrillar procollagen type I C-propeptide Homo-trimer

Released:
DOI: 10.2210/pdb5k31/pdb
PDB entry 5k31 coloured by chain, front view.
PDB entry 5k31 coloured by chain, side view.
PDB entry 5k31 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural basis of homo- and heterotrimerization of collagen I.
Sharma U, Carrique L, Vadon-Le Goff S, Mariano N, Georges RN, Delolme F, Koivunen P, Myllyharju J, Moali C, Aghajari N, Hulmes DJ
Nat Commun 8 14671 (2017)
PMID: 28281531

Function and Biology Details

Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence 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, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 255 amino acids
Theoretical weight: 28.69 KDa
Source organism: Homo sapiens
Expression system: Homo sapiens
UniProt:
  • Canonical: P02452 (Residues: 1219-1464; Coverage: 17%)
Gene name: COL1A1
Sequence domains: Fibrillar collagen C-terminal domain
Structure domains: Jelly Rolls

Ligands and Environments

3 bound ligands:
Ligand CA 6 x CA
Ligand GOL 5 x GOL
Ligand CL 3 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06DA
Spacegroup: P21
Unit cell:
a: 74.82Å b: 149.63Å c: 105.95Å
α: 90° β: 101.68° γ: 90°
R-values:
R R work R free
0.198 0.196 0.238
Expression system: Homo sapiens

Quick links

Citations

10 review citations

Sources of Collagen for Biomaterials in Skin Wound Healing.
Davison-Kotler et al. (2019)
9 more

8 mentions without citation

Structural basis of homo- and heterotrimerization of collagen I.
Sharma et al. (2017)
7 more