› 3hck

Solution NMR

NMR ensemble of the uncomplexed human HCK SH2 domain, 20 structures

Released:
DOI: 10.2210/pdb3hck/pdb
PDB entry 3hck coloured by chain, ensemble of 20 models, front view.
PDB entry 3hck coloured by chain, ensemble of 20 models, side view.
PDB entry 3hck coloured by chain, ensemble of 20 models, top view.
Source organism: Homo sapiens
Primary publication:
Sequential assignment and secondary structure determination for the Src homology 2 domain of hematopoietic cellular kinase.
Zhang W, Smithgall TE, Gmeiner WH
FEBS Lett 406 131-5 (1997)
PMID: 9109402

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: 107 amino acids
Theoretical weight: 12.24 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P08631 (Residues: 139-245; Coverage: 20%)
Gene name: HCK
Sequence domains: SH2 domain
Structure domains: SH2 domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

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

Quick links

Citations

2 citation in other articles

Crystal structure of the C-terminal SH2 domain of the p85alpha regulatory subunit of phosphoinositide 3-kinase: an SH2 domain mimicking its own substrate.
Hoedemaeker et al. (1999)
1 more

1 mention without citation

Tyrosine phosphorylation of the Lyn Src homology 2 (SH2) domain modulates its binding affinity and specificity.
Jin et al. (2015)