› 1z2f

Solution NMR

solution structure of CfAFP-501

Released:
DOI: 10.2210/pdb1z2f/pdb
PDB entry 1z2f coloured by chain, ensemble of 20 models, front view.
PDB entry 1z2f coloured by chain, ensemble of 20 models, side view.
PDB entry 1z2f coloured by chain, ensemble of 20 models, top view.
Source organism: Choristoneura fumiferana
Primary publication:
Solution structure of an antifreeze protein CfAFP-501 from Choristoneura fumiferana.
Li C, Guo X, Jia Z, Xia B, Jin C
J Biomol NMR 32 251-6 (2005)
PMID: 16132825

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-190420 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Antifreeze protein isoform 501 Chain: A
Molecule details ›
Chain: A
Length: 121 amino acids
Theoretical weight: 12.55 KDa
Source organism: Choristoneura fumiferana
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9GSA6 (Residues: 18-138; Coverage: 100%)
Sequence domains: Choristoneura fumiferana antifreeze protein (CfAFP)
Structure domains: Insect antifreeze protein

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: simulated annealing, molecular dynamics
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Mimicking biopolymers on a molecular scale: nano(bio)technology based on engineered proteins.
Grunwald et al. (2009)
3 other articles

4 mentions without citation

Insights into the Molecular Mechanisms of Alzheimer's and Parkinson's Diseases with Molecular Simulations: Understanding the Roles of Artificial and Pathological Missense Mutations in Intrinsically Disordered Proteins Related to Pathology.
Coskuner-Weber et al. (2018)
3 more