› 2kb5

Solution NMR

Solution NMR Structure of Eosinophil Cationic Protein/RNase 3

Released:
DOI: 10.2210/pdb2kb5/pdb
PDB entry 2kb5 coloured by chain, ensemble of 20 models, front view.
PDB entry 2kb5 coloured by chain, ensemble of 20 models, side view.
PDB entry 2kb5 coloured by chain, ensemble of 20 models, top view.
Source organism: Homo sapiens
Primary publication:
The (1)H, (13)C, (15)N resonance assignment, solution structure, and residue level stability of eosinophil cationic protein/RNase 3 determined by NMR spectroscopy.
Laurents DV, Bruix M, Jiménez MA, Santoro J, Boix E, Moussaoui M, Nogués MV, Rico M
Biopolymers 91 1018-28 (2009)
PMID: 19189375

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-146304 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Eosinophil cationic protein Chain: A
Molecule details ›
Chain: A
Length: 133 amino acids
Theoretical weight: 15.6 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P12724 (Residues: 28-160; Coverage: 100%)
Gene names: ECP, RNASE3, RNS3
Sequence domains: Pancreatic ribonuclease
Structure domains: Ribonuclease A-like domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: torsion angle dynamics
Expression system: Escherichia coli

Quick links

Citations

9 citation in other articles

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Mompeán et al. (2016)
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3 mentions without citation

Human antimicrobial peptides and proteins.
Wang G. (2014)
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