› 1n5p

Solution NMR

Solution structure of the cathelin-like domain of protegrins (all amide bonds involving proline residues are in trans conformation)

Released:
DOI: 10.2210/pdb1n5p/pdb
PDB entry 1n5p coloured by chain, ensemble of 15 models, front view.
PDB entry 1n5p coloured by chain, ensemble of 15 models, side view.
PDB entry 1n5p coloured by chain, ensemble of 15 models, top view.
Source organism: Sus scrofa
Primary publication:
NMR structure of the cathelin-like domain of the protegrin-3 precursor.
Yang Y, Sanchez JF, Strub MP, Brutscher B, Aumelas A
Biochemistry 42 4669-80 (2003)
PMID: 12705830

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-156096 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Protegrin-4 Chain: A
Molecule details ›
Chain: A
Length: 105 amino acids
Theoretical weight: 11.74 KDa
Source organism: Sus scrofa
Expression system: Escherichia coli
UniProt:
  • Canonical: P49933 (Residues: 30-130; Coverage: 84%)
Gene name: NPG4
Sequence domains: Cathelicidin
Structure domains: Nuclear Transport Factor 2; Chain: A,

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: distance geometry and simulated annealing
Expression system: Escherichia coli

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Citations

2 review citations

Bone morphogenetic protein-2 activity is regulated by secreted phosphoprotein-24 kd, an extracellular pseudoreceptor, the gene for which maps to a region of the human genome important for bone quality.
Brochmann et al. (2009)
1 more