4OMO: C-Src tyrosine kinase SH3 domain mutant Q128E

Crystal structure of the c-Src tyrosine kinase SH3 domain mutant Q128E. Determined by X-ray diffraction at 1.04 Å resolution. Released 10 Dec 2014.

Method
X-ray diffraction
Resolution
1.04 Å
Organism
Gallus gallus
Chains
2
Atoms
1,175
Mol. weight
14.17 kDa
Ligands
NI
Released
10 Dec 2014

Explore 4OMO in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4OMO contains 3 α-helices and 16 β-strands across 2 chains. 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-strand86-8831
β-strand9212
β-strand9911
α-helix100-1012
β-strand10212
β-strand107-11261
β-strand118-12361
β-strand129-13351
α-helix134-1363
β-strand137-13931
Chain B: 1 helix, 8 β-strands
ElementResiduesLengthSheet
β-strand85-8843
β-strand9214
β-strand9913
β-strand10214
β-strand107-11043
β-strand118-12363
β-strand129-13353
α-helix134-1363
β-strand137-13933

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Proto-oncogene tyrosine-protein kinase SrcA, Bprotein61Gallus gallusP00523 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>4OMO_1 Proto-oncogene tyrosine-protein kinase Src (chains A, B)
GSHMTFVALYDYESRTETDLSFKKGERLQIVNNTEGDWWLAHSLTTGETGYIPSNYVAPS
D

Ligands and cofactors

IDNameFormulaCopies
NINickel (II) ionNi2

Water and common crystallization additives (EPE) are not listed.

Primary 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, J., Martinez-Rodriguez, S., Martin-Garcia, J.M. et al. PLoS One (2014) 9:e113224-e113224. DOI 10.1371/journal.pone.0113224 · PubMed

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

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