› 4hvv

X-ray diffraction
1.1Å resolution

Crystal structure of the T98E c-Src-SH3 domain mutant in complex with the high affinity peptide APP12

Released:
DOI: 10.2210/pdb4hvv/pdb
PDB entry 4hvv coloured by chain, front view.
PDB entry 4hvv coloured by chain, side view.
PDB entry 4hvv coloured by chain, top view.
Source organism: Gallus gallus
Primary publication:
Atomic resolution structures of the c-Src SH3 domain in complex with two high-affinity peptides from classes I and II.
Bacarizo J, Camara-Artigas A
Acta Crystallogr D Biol Crystallogr 69 756-66 (2013)
PMID: 23633584

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:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-132642 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Proto-oncogene tyrosine-protein kinase Src Chain: A
Molecule details ›
Chain: A
Length: 60 amino acids
Theoretical weight: 6.85 KDa
Source organism: Gallus gallus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P00523 (Residues: 85-140; Coverage: 11%)
Gene name: SRC
Sequence domains: SH3 domain
Structure domains: SH3 Domains
SYNTHETIC PEPTIDE Acetyl-APPLPPRNRP Chain: B
Molecule details ›
Chain: B
Length: 11 amino acids
Theoretical weight: 1.14 KDa
Source organism: Gallus gallus
Expression system: Not provided

Ligands and Environments

1 bound ligand:
Ligand SO4 1 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-4
Spacegroup: P3121
Unit cell:
a: 31.588Å b: 31.588Å c: 106.689Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.144 0.144 0.156
Expression systems:
  • Escherichia coli BL21(DE3)
  • Not provided

Quick links

Citations

1 review citation

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

2 mentions without citation

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 et al. (2014)
1 more