› 4ae2

X-ray diffraction
1.68Å resolution

Crystal structure of Human fibrillar procollagen type III C- propeptide trimer

Released:
DOI: 10.2210/pdb4ae2/pdb
PDB entry 4ae2 coloured by chain, front view.
PDB entry 4ae2 coloured by chain, side view.
PDB entry 4ae2 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural basis of fibrillar collagen trimerization and related genetic disorders.
Bourhis JM, Mariano N, Zhao Y, Harlos K, Exposito JY, Jones EY, Moali C, Aghajari N, Hulmes DJ
Nat Struct Mol Biol 19 1031-6 (2012)
PMID: 23001006

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-135859 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Collagen alpha-1(III) chain Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 256 amino acids
Theoretical weight: 28.82 KDa
Source organism: Homo sapiens
Expression system: Homo sapiens
UniProt:
  • Canonical: P02461 (Residues: 1222-1466; Coverage: 17%)
Gene name: COL3A1
Sequence domains: Fibrillar collagen C-terminal domain
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand CA 3 x CA
Ligand NO3 5 x NO3
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I03
Spacegroup: P212121
Unit cell:
a: 76.45Å b: 90.36Å c: 102.44Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.164 0.161 0.214
Expression system: Homo sapiens

Quick links

Citations

17 review citations

Extracellular matrix assembly: a multiscale deconstruction.
Mouw et al. (2014)
16 more

8 mentions without citation

Structural basis of fibrillar collagen trimerization and related genetic disorders.
Bourhis et al. (2012)
7 more