› 4omo

X-ray diffraction
1.04Å resolution

Crystal structure of the c-Src tyrosine kinase SH3 domain mutant Q128E

Released:
DOI: 10.2210/pdb4omo/pdb
PDB entry 4omo coloured by chain, front view.
PDB entry 4omo coloured by chain, side view.
PDB entry 4omo coloured by chain, top view.
Source organism: Gallus gallus
Primary publication:
Electrostatic effects in the folding of the SH3 domain of the c-Src tyrosine kinase: pH-dependence in 3D-domain swapping and amyloid formation.
Bacarizo J, Martinez-Rodriguez S, Martin-Garcia JM, Andujar-Sanchez M, Ortiz-Salmeron E, Neira JL, Camara-Artigas A
PLoS One 9 e113224 (2014)
PMID: 25490095

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 analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-132629 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Proto-oncogene tyrosine-protein kinase Src Chains: A, B
Molecule details ›
Chains: A, B
Length: 61 amino acids
Theoretical weight: 6.91 KDa
Source organism: Gallus gallus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P00523 (Residues: 85-141; Coverage: 11%)
Gene name: SRC
Sequence domains: SH3 domain
Structure domains: SH3 Domains

Ligands and Environments

2 bound ligands:
Ligand NI 2 x NI
Ligand EPE 1 x EPE
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALBA BEAMLINE XALOC
Spacegroup: P212121
Unit cell:
a: 43.711Å b: 45.464Å c: 57.807Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.149 0.148 0.168
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

1 review citation

Crystallographic studies on protein misfolding: Domain swapping and amyloid formation in the SH3 domain.
Cámara-Artigas A. (2016)
6 other articles

4 mentions without citation

Utility of Covalent Labeling Mass Spectrometry Data in Protein Structure Prediction with Rosetta.
Aprahamian et al. (2019)
3 more