› 2lx2

Solution NMR

1H,13C,15N assignments for an isoform of the type III antifreeze protein from notched-fin eelpout

Released:
DOI: 10.2210/pdb2lx2/pdb
PDB entry 2lx2 coloured by chain, ensemble of 20 models, front view.
PDB entry 2lx2 coloured by chain, ensemble of 20 models, side view.
PDB entry 2lx2 coloured by chain, ensemble of 20 models, top view.
Source organism: Zoarces elongatus
Primary publication:
NMR structure note: a defective isoform and its activity-improved variant of a type III antifreeze protein from Zoarces elongates Kner.
Kumeta H, Ogura K, Nishimiya Y, Miura A, Inagaki F, Tsuda S
J Biomol NMR 55 225-30 (2013)
PMID: 23288342

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-176124 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ice-structuring protein Chain: A
Molecule details ›
Chain: A
Length: 67 amino acids
Theoretical weight: 7.07 KDa
Source organism: Zoarces elongatus
Expression system: Escherichia coli
UniProt:
  • Canonical: Q53UI9 (Residues: 23-88; Coverage: 100%)
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
Chemical shift assignment: 97%
Refinement method: distance geometry, simulated annealing, torsion angle dynamics
Expression system: Escherichia coli

Quick links

Citations

5 citation in other articles

Prolonging hypothermic storage (4 C) of bovine embryos with fish antifreeze protein.
Ideta et al. (2015)
4 more

1 mention without citation

Molecular basis of ice-binding and cryopreservation activities of type III antifreeze proteins.
Choi et al. (2021)