› 1csz

Solution NMR

SYK TYROSINE KINASE C-TERMINAL SH2 DOMAIN COMPLEXED WITH A PHOSPHOPEPTIDEFROM THE GAMMA CHAIN OF THE HIGH AFFINITY IMMUNOGLOBIN G RECEPTOR, NMR

Released:
DOI: 10.2210/pdb1csz/pdb
PDB entry 1csz coloured by chain, front view.
PDB entry 1csz coloured by chain, side view.
PDB entry 1csz coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Solution structure of the C-terminal SH2 domain of the human tyrosine kinase Syk complexed with a phosphotyrosine pentapeptide.
Narula SS, Yuan RW, Adams SE, Green OM, Green J, Philips TB, Zydowsky LD, Botfield MC, Hatada M, Laird ER
Structure 3 1061-73 (1995)
PMID: 8590001

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:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-155058 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Tyrosine-protein kinase SYK Chain: A
Molecule details ›
Chain: A
Length: 112 amino acids
Theoretical weight: 12.73 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P43405 (Residues: 162-265; Coverage: 16%)
Gene name: SYK
Sequence domains: SH2 domain
Structure domains: SH2 domain
ACETYL-THR-PTR-GLU-THR-LEU-NH2 Chain: B
Molecule details ›
Chain: B
Length: 7 amino acids
Theoretical weight: 730 Da
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

6 review citations

Fc receptor biology.
Daëron M. (1997)
5 more

1 mention without citation

Molecular modeling of retinoschisin with functional analysis of pathogenic mutations from human X-linked retinoschisis.
Sergeev et al. (2010)