› 1tze

X-ray diffraction
2.1Å resolution

SIGNAL TRANSDUCTION ADAPTOR GROWTH FACTOR, GRB2 SH2 DOMAIN COMPLEXED WITH PHOSPHOTYROSYL HEPTAPEPTIDE LYS-PRO-PHE-PTYR-VAL-ASN-VAL-NH2 (KFPPYVNC-NH2)

Released:
DOI: 10.2210/pdb1tze/pdb
PDB entry 1tze coloured by chain, front view.
PDB entry 1tze coloured by chain, side view.
PDB entry 1tze coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural basis for specificity of Grb2-SH2 revealed by a novel ligand binding mode.
Rahuel J, Gay B, Erdmann D, Strauss A, Garcia-Echeverría C, Furet P, Caravatti G, Fretz H, Schoepfer J, Grütter MG
Nat Struct Biol 3 586-9 (1996)
PMID: 8673601

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assemblies composition:
hetero dimer (preferred)
hetero tetramer
Assembly name:
PDBe Complex ID:
PDB-CPX-158857 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Growth factor receptor-bound protein 2 Chain: E
Molecule details ›
Chain: E
Length: 98 amino acids
Theoretical weight: 11.45 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P62993 (Residues: 55-152; Coverage: 45%)
Gene names: ASH, GRB2
Sequence domains: SH2 domain
Structure domains: SH2 domain
PHOSPHOTYROSYL HEPTAPEPTIDE LYS-PRO-PHE-PTYR-VAL-ASN-VAL-NH2 Chain: I
Molecule details ›
Chain: I
Length: 8 amino acids
Theoretical weight: 945 Da
Source organism: Homo sapiens
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: P41212
Unit cell:
a: 50.3Å b: 50.3Å c: 89.9Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.203 0.203 not available
Expression systems:
  • Escherichia coli BL21(DE3)
  • Not provided

Quick links

Citations

21 review citations

Modular peptide recognition domains in eukaryotic signaling.
Kuriyan et al. (1997)
20 more

16 mentions without citation

Tandem domain swapping: determinants of multidomain protein misfolding.
Lafita et al. (2019)
15 more