› 1fmk

X-ray diffraction
1.5Å resolution

CRYSTAL STRUCTURE OF HUMAN TYROSINE-PROTEIN KINASE C-SRC

Released:
DOI: 10.2210/pdb1fmk/pdb
PDB entry 1fmk coloured by chain, front view.
PDB entry 1fmk coloured by chain, side view.
PDB entry 1fmk coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Three-dimensional structure of the tyrosine kinase c-Src.
Xu W, Harrison SC, Eck MJ
Nature 385 595-602 (1997)
PMID: 9024657

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 domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-146379 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Proto-oncogene tyrosine-protein kinase Src Chain: A
Molecule details ›
Chain: A
Length: 452 amino acids
Theoretical weight: 51.71 KDa
Source organism: Homo sapiens
Expression system: unidentified baculovirus
UniProt:
  • Canonical: P12931 (Residues: 86-536; Coverage: 84%)
Gene names: SRC, SRC1
Sequence domains:
Structure domains:

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
Spacegroup: P212121
Unit cell:
a: 51.759Å b: 87.38Å c: 101.295Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.21 0.21 0.264
Expression system: unidentified baculovirus

Quick links

Citations

193 review citations

Free radicals in the physiological control of cell function.
Dröge W. (2002)
192 more

89 mentions without citation

Mechanisms of drug resistance in kinases.
Barouch-Bentov et al. (2011)
88 more