› 1bbz

X-ray diffraction
1.65Å resolution

CRYSTAL STRUCTURE OF THE ABL-SH3 DOMAIN COMPLEXED WITH A DESIGNED HIGH-AFFINITY PEPTIDE LIGAND: IMPLICATIONS FOR SH3-LIGAND INTERACTIONS

Released:
DOI: 10.2210/pdb1bbz/pdb
PDB entry 1bbz coloured by chain, front view.
PDB entry 1bbz coloured by chain, side view.
PDB entry 1bbz coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Crystal structure of the abl-SH3 domain complexed with a designed high-affinity peptide ligand: implications for SH3-ligand interactions.
Pisabarro MT, Serrano L, Wilmanns M
J Mol Biol 281 513-21 (1998)
PMID: 9698566

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 domain:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-132605 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Tyrosine-protein kinase ABL1 Chains: A, C, E, G
Molecule details ›
Chains: A, C, E, G
Length: 58 amino acids
Theoretical weight: 6.42 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P00519 (Residues: 64-121; Coverage: 5%)
Gene names: ABL, ABL1, JTK7
Sequence domains: SH3 domain
Structure domains: SH3 Domains
PEPTIDE P41 Chains: B, D, F, H
Molecule details ›
Chains: B, D, F, H
Length: 11 amino acids
Theoretical weight: 1.04 KDa
Source organism: Homo sapiens
Expression system: Not provided

Ligands and Environments

1 bound ligand:
Ligand SO4 4 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE BW7B
Spacegroup: P212121
Unit cell:
a: 46.68Å b: 73.79Å c: 80Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.205 0.205 0.266
Expression systems:
  • Escherichia coli
  • Not provided

Quick links

Citations

8 review citations

Recognition of proline-rich motifs by protein-protein-interaction domains.
Ball et al. (2005)
7 more

36 mentions without citation

Noise in cellular signaling pathways: causes and effects.
Ladbury et al. (2012)
35 more