› 1h92

Solution NMR

SH3 domain of human Lck tyrosine kinase

Released:
DOI: 10.2210/pdb1h92/pdb
PDB entry 1h92 coloured by chain, ensemble of 30 models, front view.
PDB entry 1h92 coloured by chain, ensemble of 30 models, side view.
PDB entry 1h92 coloured by chain, ensemble of 30 models, top view.
Source organism: Homo sapiens
Primary publication:
Structural investigation of the binding of a herpesviral protein to the SH3 domain of tyrosine kinase Lck.
Schweimer K, Hoffmann S, Bauer F, Friedrich U, Kardinal C, Feller SM, Biesinger B, Sticht H
Biochemistry 41 5120-30 (2002)
PMID: 11955060

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-138948 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Tyrosine-protein kinase Lck Chain: A
Molecule details ›
Chain: A
Length: 63 amino acids
Theoretical weight: 7.01 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P06239 (Residues: 58-120; Coverage: 12%)
Gene name: LCK
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: AB INITIO SIMULATED ANNEALING
Expression system: Escherichia coli BL21

Quick links

Citations

3 review citations

Specificity and versatility of SH3 and other proline-recognition domains: structural basis and implications for cellular signal transduction.
Li SS. (2005)
2 more

3 mentions without citation

The effects of rigid motions on elastic network model force constants.
Lezon TR. (2012)
2 more