› 2llt

Solution NMR

Post-translational S-nitrosylation is an endogenous factor fine-tuning human S100A1 protein properties

Released:
DOI: 10.2210/pdb2llt/pdb
PDB entry 2llt coloured by chain, ensemble of 20 models, front view.
PDB entry 2llt coloured by chain, ensemble of 20 models, side view.
PDB entry 2llt coloured by chain, ensemble of 20 models, top view.
Source organism: Homo sapiens
Primary publication:
Post-translational S-nitrosylation is an endogenous factor fine tuning the properties of human S100A1 protein.
Lenarčič Živković M, Zaręba-Kozioł M, Zhukova L, Poznański J, Zhukov I, Wysłouch-Cieszyńska A
J Biol Chem 287 40457-70 (2012)
PMID: 22989881

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-149925 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Protein S100-A1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 93 amino acids
Theoretical weight: 10.45 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P23297 (Residues: 2-94; Coverage: 99%)
Gene names: S100A, S100A1
Sequence domains:
Structure domains: EF-hand

Ligands and Environments

No bound ligands
1 modified residue:
Ligand SNC 2 x SNC

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 44%
Refinement method: simulated annealing
Expression system: Escherichia coli

Quick links

Citations

4 review citations

Protein post-translational modifications: In silico prediction tools and molecular modeling.
Audagnotto et al. (2017)
3 more

5 mentions without citation

dbSNO 2.0: a resource for exploring structural environment, functional and disease association and regulatory network of protein S-nitrosylation.
Chen et al. (2015)
4 more