› 1shb

X-ray diffraction
2Å resolution

CRYSTAL STRUCTURE OF THE PHOSPHOTYROSINE RECOGNITION DOMAIN SH2 OF V-SRC COMPLEXED WITH TYROSINE-PHOSPHORYLATED PEPTIDES

Released:
DOI: 10.2210/pdb1shb/pdb
PDB entry 1shb coloured by chain, front view.
PDB entry 1shb coloured by chain, side view.
PDB entry 1shb coloured by chain, top view.
Source organism: Rous sarcoma virus
Primary publication:
Crystal structure of the phosphotyrosine recognition domain SH2 of v-src complexed with tyrosine-phosphorylated peptides.
Waksman G, Kominos D, Robertson SC, Pant N, Baltimore D, Birge RB, Cowburn D, Hanafusa H, Mayer BJ, Overduin M, Resh MD, Rios CB, Silverman L, Kuriyan J
Nature 358 646-53 (1992)
PMID: 1379696

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-132666 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Tyrosine-protein kinase transforming protein Src Chain: A
Molecule details ›
Chain: A
Length: 104 amino acids
Theoretical weight: 11.97 KDa
Source organism: Rous sarcoma virus
Expression system: Not provided
UniProt:
  • Canonical: P00524 (Residues: 144-247; Coverage: 20%)
Gene name: V-SRC
Sequence domains: SH2 domain
Structure domains: SH2 domain
PHOSPHOPEPTIDE B Chain: B
Molecule details ›
Chain: B
Length: 5 amino acids
Theoretical weight: 702 Da
Source organism: Rous sarcoma virus
Expression system: Not provided

Ligands and Environments

No bound ligands
1 modified residue:
Ligand PTR 1 x PTR

Experiments and Validation Details

Entry percentile scores
Spacegroup: P41
Unit cell:
a: 47.9Å b: 47.9Å c: 53.4Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.19 0.19 not available
Expression system: Not provided

Quick links

Citations

74 review citations

PAS domains: internal sensors of oxygen, redox potential, and light.
Taylor et al. (1999)
73 more

2 mentions without citation

Structure of a novel phosphotyrosine-binding domain in Hakai that targets E-cadherin.
Mukherjee et al. (2012)
1 more