1ABO: Abl tyrosine kinase

Crystal structure of the complex of the abl tyrosine kinase SH3 domain with 3BP-1 synthetic peptide. Determined by X-ray diffraction at 2.0 Å resolution. Released 15 Oct 1995.

Method
X-ray diffraction
Resolution
2.0 Å
Organism
Mus musculus
Chains
4
Atoms
1,181
Mol. weight
15.99 kDa
Released
15 Oct 1995

Explore 1ABO in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1ABO contains 4 α-helices and 16 β-strands across 4 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.

Chains A and B: 1 helix, 8 β-strands

ElementResiduesLengthSheet
β-strand65-6841
β-strand7212
β-strand7911
β-strand8212
β-strand87-9371
β-strand99-10461
β-strand107-11261
α-helix113-1153
β-strand116-11831
Chains C and D: 1 helix, 0 β-strands
ElementResiduesLengthSheet
α-helix5-95

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Abl tyrosine kinaseA, Bprotein62Mus musculusP00520 (AlphaFold model)
3BP-1 synthetic peptide, 10 residuesC, Dprotein10P55194 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>1ABO_1 ABL TYROSINE KINASE (chains A, B)
MNDPNLFVALYDFVASGDNTLSITKGEKLRVLGYNHNGEWCEAQTKNGQGWVPSNYITPV
NS
Sequence of entity 2 (C, D), FASTA
>1ABO_2 3BP-1 SYNTHETIC PEPTIDE, 10 RESIDUES (chains C, D)
APTMPPPLPP

Primary citation

High-resolution crystal structures of tyrosine kinase SH3 domains complexed with proline-rich peptides. Musacchio, A., Saraste, M., Wilmanns, M. Nat Struct Biol (1994) 1:546-551. DOI 10.1038/nsb0894-546 · PubMed

Other PDB entries of the same protein (UniProt P00520 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

About this viewer

MolViewer shows 1ABO 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.