› 2l0p

Solution NMR

Solution structure of human apo-S100A1 protein by NMR spectroscopy

Released:
DOI: 10.2210/pdb2l0p/pdb
PDB entry 2l0p coloured by chain, ensemble of 20 models, front view.
PDB entry 2l0p coloured by chain, ensemble of 20 models, side view.
PDB entry 2l0p coloured by chain, ensemble of 20 models, top view.
Source organism: Homo sapiens
Primary publication:
Solution NMR structure and dynamics of human apo-S100A1 protein.
Nowakowski M, Jaremko ��, Jaremko M, Zhukov I, Belczyk A, Bierzy��ski A, Ejchart A
J. Struct. Biol. 174 391-9 (2011)
PMID: 21296671

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: 94 amino acids
Theoretical weight: 10.56 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P23297 (Residues: 1-94; Coverage: 100%)
Gene names: S100A, S100A1
Sequence domains:
Structure domains: EF-hand

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

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

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Citations

7 citation in other articles

Post-translational S-nitrosylation is an endogenous factor fine tuning the properties of human S100A1 protein.
Lenarčič Živković et al. (2012)
6 more

7 mentions without citation

Sequence signatures of direct complementarity between mRNAs and cognate proteins on multiple levels.
Hlevnjak et al. (2012)
6 more