6XX4: C-Src SH3 domain H122R-Q128E mutant

Crystal structure of the c-Src SH3 domain H122R-Q128E mutant in complex with Ni(II) at pH 7.5 co-crystallized with methyl beta-cyclodextrin. Determined by X-ray diffraction at 1.05 Å resolution. Released 22 Apr 2020.

Method
X-ray diffraction
Resolution
1.05 Å
Organism
Gallus gallus
Chains
1
Atoms
575
Mol. weight
8.24 kDa
Ligands
NI
Released
22 Apr 2020

Explore 6XX4 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6XX4 contains 2 α-helices and 8 β-strands across 1 chain. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 2 helices, 8 β-strands

ElementResiduesLengthSheet
β-strand85-8841
β-strand9212
β-strand9911
α-helix100-1012
β-strand10212
β-strand107-11041
β-strand118-12361
β-strand129-13351
α-helix134-1363
β-strand137-13931

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Proto-oncogene tyrosine-protein kinase SrcAprotein61Gallus gallusP00523 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>6XX4_1 Proto-oncogene tyrosine-protein kinase Src (chains A)
GSHMTFVALYDYESRTETDLSFKKGERLQIVNNTEGDWWLARSLTTGETGYIPSNYVAPS
D

Ligands and cofactors

IDNameFormulaCopies
NINickel (II) ionNi1

Primary citation

The effect of an engineered ATCUN motif on the structure and biophysical properties of the SH3 domain of c-Src tyrosine kinase. Plaza-Garrido, M., Salinas-Garcia, M.C., Martinez, J.C. et al. J Biol Inorg Chem (2020) 25:621-634. DOI 10.1007/s00775-020-01785-0 · PubMed

Other PDB entries of the same protein (UniProt P00523 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

About this viewer

MolViewer shows 6XX4 directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.