› 1byg

X-ray diffraction
2.4Å resolution

KINASE DOMAIN OF HUMAN C-TERMINAL SRC KINASE (CSK) IN COMPLEX WITH INHIBITOR STAUROSPORINE

Released:
DOI: 10.2210/pdb1byg/pdb
PDB entry 1byg coloured by chain, front view.
PDB entry 1byg coloured by chain, side view.
PDB entry 1byg coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structure of the protein tyrosine kinase domain of C-terminal Src kinase (CSK) in complex with staurosporine.
Lamers MB, Antson AA, Hubbard RE, Scott RK, Williams DH
J Mol Biol 285 713-25 (1999)
PMID: 9878439

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-154353 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Tyrosine-protein kinase CSK Chain: A
Molecule details ›
Chain: A
Length: 278 amino acids
Theoretical weight: 31.18 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P41240 (Residues: 173-450; Coverage: 62%)
Gene name: CSK
Sequence domains: Protein tyrosine and serine/threonine kinase
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand STU 1 x STU
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P21212
Unit cell:
a: 44.49Å b: 120.58Å c: 48.29Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.199 0.199 0.287
Expression system: Escherichia coli

Quick links

Citations

20 review citations

Regulation of protein kinases; controlling activity through activation segment conformation.
Nolen et al. (2004)
19 more

19 mentions without citation

Kinase packing defects as drug targets.
Crespo et al. (2007)
18 more