› 2ka3

Solution NMR

Structure of EMILIN-1 C1Q-like domain

Released:
DOI: 10.2210/pdb2ka3/pdb
PDB entry 2ka3 coloured by chain, ensemble of 10 models, front view.
PDB entry 2ka3 coloured by chain, ensemble of 10 models, side view.
PDB entry 2ka3 coloured by chain, ensemble of 10 models, top view.
Source organism: Homo sapiens
Primary publication:
NMR-based homology model for the solution structure of the C-terminal globular domain of EMILIN1.
Verdone G, Corazza A, Colebrooke SA, Cicero D, Eliseo T, Boyd J, Doliana R, Fogolari F, Viglino P, Colombatti A, Campbell ID, Esposito G
J Biomol NMR 43 79-96 (2009)
PMID: 19023665

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-195352 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
EMILIN-1 Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 162 amino acids
Theoretical weight: 17.23 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9Y6C2 (Residues: 867-1016; Coverage: 15%)
Gene names: EMI, EMILIN1
Sequence domains: C1q domain
Structure domains: Jelly Rolls

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: simulated annealing, restrained energy minimization
Expression system: Escherichia coli

Quick links

Citations

1 review citation

The crucial role of trimerization domains in collagen folding.
Boudko et al. (2012)
5 other articles

2 mentions without citation

The dipeptidyl peptidase IV inhibitors vildagliptin and K-579 inhibit a phospholipase C: a case of promiscuous scaffolds in proteins.
Chakraborty et al. (2013)
1 more