› 1uuc

Solution NMR

solution structure of a chimeric LEKTI-domain

Released:
DOI: 10.2210/pdb1uuc/pdb
PDB entry 1uuc coloured by chain, ensemble of 30 models, front view.
PDB entry 1uuc coloured by chain, ensemble of 30 models, side view.
PDB entry 1uuc coloured by chain, ensemble of 30 models, top view.
Source organism: Homo sapiens
Primary publication:
The solution structure of a chimeric LEKTI domain reveals a chameleon sequence.
Tidow H, Lauber T, Vitzithum K, Sommerhoff CP, Rösch P, Marx UC
Biochemistry 43 11238-47 (2004)
PMID: 15366933

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domain:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-192495 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Hemofiltrate peptide HF6478 Chain: A
Molecule details ›
Chain: A
Length: 55 amino acids
Theoretical weight: 6.41 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9NQ38 (Residues: 23-77; Coverage: 5%)
Gene name: SPINK5
Structure domains: Wheat Germ Agglutinin (Isolectin 2); domain 1

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 46%
Refinement method: simulated annealing
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Pathological unfoldomics of uncontrolled chaos: intrinsically disordered proteins and human diseases.
Uversky et al. (2014)
1 more

1 mention 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)