› 2n04

Solution NMR

Solution Structure of the phosphorylated N-terminal region of Human Cysteine String Protein (CSP)

Released:
DOI: 10.2210/pdb2n04/pdb
PDB entry 2n04 coloured by chain, ensemble of 20 models, front view.
PDB entry 2n04 coloured by chain, ensemble of 20 models, side view.
PDB entry 2n04 coloured by chain, ensemble of 20 models, top view.
Source organism: Homo sapiens
Primary publication:
Phosphorylation of Cysteine String Protein Triggers a Major Conformational Switch.
Patel P, Prescott GR, Burgoyne RD, Lian LY, Morgan A
Structure 24 1380-1386 (2016)
PMID: 27452402

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-190594 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
DnaJ homolog subfamily C member 5 Chain: A
Molecule details ›
Chain: A
Length: 105 amino acids
Theoretical weight: 11.98 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9H3Z4 (Residues: 1-100; Coverage: 51%)
Gene names: CLN4, DNAJC5
Sequence domains: DnaJ domain
Structure domains: DnaJ domain

Ligands and Environments

No bound ligands
1 modified residue:
Ligand SEP 1 x SEP

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 88%
Refinement method: simulated annealing
Expression system: Escherichia coli

Quick links

Citations

5 review citations

The Complex Phosphorylation Patterns that Regulate the Activity of Hsp70 and Its Cochaperones.
Velasco et al. (2019)
4 more

4 mentions without citation

The Role of Co-chaperones in Synaptic Proteostasis and Neurodegenerative Disease.
Gorenberg et al. (2017)
3 more