› 5hck

Solution NMR

HUMAN HCK SH3 DOMAIN, NMR, MINIMIZED AVERAGE STRUCTURE

Released:
DOI: 10.2210/pdb5hck/pdb
PDB entry 5hck coloured by chain, front view.
PDB entry 5hck coloured by chain, side view.
PDB entry 5hck coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Solution structure of the human Hck SH3 domain and identification of its ligand binding site.
Horita DA, Baldisseri DM, Zhang W, Altieri AS, Smithgall TE, Gmeiner WH, Byrd RA
J Mol Biol 278 253-65 (1998)
PMID: 9571048

Function and Biology Details

Reaction catalysed: 
ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-140247 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Tyrosine-protein kinase HCK Chain: A
Molecule details ›
Chain: A
Length: 72 amino acids
Theoretical weight: 8.24 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P08631 (Residues: 72-143; Coverage: 14%)
Gene name: HCK
Sequence domains: SH3 domain
Structure domains: SH3 Domains

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

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

Quick links

Citations

1 review citation

SH3 domains: modules of protein-protein interactions.
Kurochkina et al. (2013)
12 other articles

4 mentions without citation

NextGen protein design.
Sawyer et al. (2013)
3 more