› 3n3f

X-ray diffraction
2Å resolution

Crystal Structure of the Human Collagen XV Trimerization Domain: A Potent Trimerizing Unit Common to Multiplexin Collagens

Released:
DOI: 10.2210/pdb3n3f/pdb
PDB entry 3n3f coloured by chain, front view.
PDB entry 3n3f coloured by chain, side view.
PDB entry 3n3f coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Crystal structure of the human collagen XV trimerization domain: a potent trimerizing unit common to multiplexin collagens.
Wirz JA, Boudko SP, Lerch TF, Chapman MS, Bächinger HP
Matrix Biol 30 9-15 (2011)
PMID: 20932905

Function and Biology Details

Biochemical function:
  • not assigned
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-153813 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Collagen alpha-1(XV) chain Chains: A, B
Molecule details ›
Chains: A, B
Length: 54 amino acids
Theoretical weight: 6.26 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P39059 (Residues: 1133-1186; Coverage: 4%)
Gene name: COL15A1
Sequence domains: Collagen trimerization domain
Structure domains: YefM-like fold

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P63
Unit cell:
a: 49.12Å b: 49.12Å c: 65.6Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.216 0.216 0.25
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

3 review citations

The crucial role of trimerization domains in collagen folding.
Boudko et al. (2012)
2 more

4 mentions without citation

Neutralization of SARS-CoV-2 by highly potent, hyperthermostable, and mutation-tolerant nanobodies.
Güttler et al. (2021)
3 more