› 5cdw

X-ray diffraction
2.6Å resolution

Crystal Structure Analysis of a mutant Grb2 SH2 domain (W121G) with a pYVNV peptide

Released:
DOI: 10.2210/pdb5cdw/pdb
PDB entry 5cdw coloured by chain, front view.
PDB entry 5cdw coloured by chain, side view.
PDB entry 5cdw coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural and biophysical investigation of the interaction of a mutant Grb2 SH2 domain (W121G) with its cognate phosphopeptide.
Papaioannou D, Geibel S, Kunze MB, Kay CW, Waksman G
Protein Sci 25 627-37 (2016)
PMID: 26645482

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-158887 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Growth factor receptor-bound protein 2 Chains: A, B, C, E, G, H, K, L, O, P, U, V, Y, Z, c, d
Molecule details ›
Chains: A, B, C, E, G, H, K, L, O, P, U, V, Y, Z, c, d
Length: 100 amino acids
Theoretical weight: 11.58 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P62993 (Residues: 54-153; Coverage: 46%)
Gene names: ASH, GRB2
Sequence domains: SH2 domain
Structure domains: SH2 domain
SER-PTR-VAL-ASN-VAL-GLN Chains: D, F, I, J, M, N, Q, R, T, X, a, b, f, h, j, s
Molecule details ›
Chains: D, F, I, J, M, N, Q, R, T, X, a, b, f, h, j, s
Length: 6 amino acids
Theoretical weight: 789 Da
Source organism: Homo sapiens
Expression system: Not provided

Ligands and Environments

No bound ligands
1 modified residue:
Ligand PTR 16 x PTR

Experiments and Validation Details

Entry percentile scores
X-ray source: SOLEIL BEAMLINE PROXIMA 1
Spacegroup: P21
Unit cell:
a: 82.65Å b: 72.14Å c: 172.14Å
α: 90° β: 93.31° γ: 90°
R-values:
R R work R free
0.239 0.236 0.294
Expression systems:
  • Escherichia coli
  • Not provided

Quick links

Citations

4 review citations

(S)Pinning down protein interactions by NMR.
Teilum et al. (2017)
3 more