7vvg

X-ray diffraction
1.7Å resolution

Crystal Structure of HRasG12V(GMPPNP-bound) in complex with the Ras-binding domain(RBD) of SIN1

Released:
Source organism: Homo sapiens
Primary publication:
Structural insights into Ras regulation by SIN1.
Proc. Natl. Acad. Sci. U.S.A. 119 e2119990119-e2119990119 (2022)
PMID: 35522713

Function and Biology Details

Reaction catalysed:
GTP + H(2)O = GDP + phosphate
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
GTPase HRas, N-terminally processed Chain: A
Molecule details ›
Chain: A
Length: 166 amino acids
Theoretical weight: 18.92 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P01112 (Residues: 1-166; Coverage: 88%)
Gene names: HRAS, HRAS1
Sequence domains: Ras family
Target of rapamycin complex 2 subunit MAPKAP1 Chain: C
Molecule details ›
Chain: C
Length: 87 amino acids
Theoretical weight: 9.81 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9BPZ7 (Residues: 274-360; Coverage: 17%)
Gene names: MAPKAP1, MIP1, SIN1

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRF BEAMLINE BL19U1
Spacegroup: P6122
Unit cell:
a: 101.032Å b: 101.032Å c: 124.208Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.179 0.178 0.202
Expression system: Escherichia coli