› 1c89

Solution NMR

NMR STRUCTURE OF INTRAMOLECULAR DIMER ANTIFREEZE PROTEIN RD3, 40 SA STRUCTURES

Released:
DOI: 10.2210/pdb1c89/pdb
PDB entry 1c89 coloured by chain, ensemble of 40 models, front view.
PDB entry 1c89 coloured by chain, ensemble of 40 models, side view.
PDB entry 1c89 coloured by chain, ensemble of 40 models, top view.
Source organism: Pachycara brachycephalum
Primary publication:
NMR analysis of type III antifreeze protein intramolecular dimer. Structural basis for enhanced activity.
Miura K, Ohgiya S, Hoshino T, Nemoto N, Suetake T, Miura A, Spyracopoulos L, Kondo H, Tsuda S
J Biol Chem 276 1304-10 (2001)
PMID: 11010977

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-153014 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ice-structuring protein RD3 Chain: A
Molecule details ›
Chain: A
Length: 134 amino acids
Theoretical weight: 14.49 KDa
Source organism: Pachycara brachycephalum
Expression system: Escherichia coli
UniProt:
  • Canonical: P35753 (Residues: 1-134; Coverage: 100%)
Sequence domains: SAF domain
Structure domains: Antifreeze-like/N-acetylneuraminic acid synthase C-terminal domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: SA
Expression system: Escherichia coli

Quick links

Citations

3 review citations

Antifreeze proteins: an unusual receptor-ligand interaction.
Jia et al. (2002)
2 more

1 mention without citation

Identification of antifreeze proteins and their functional residues by support vector machine and genetic algorithms based on n-peptide compositions.
Yu et al. (2011)