6a9y

X-ray diffraction
2.7Å resolution

The crystal structure of Mu homology domain of SGIP1

Released:
Source organism: Homo sapiens
Primary publication:
SGIP1 dimerizes via intermolecular disulfide bond in μHD domain during cellular endocytosis.
Biochem Biophys Res Commun 505 99-105 (2018)
PMID: 30236986

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
PDBe Complex ID:
PDB-CPX-189676 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
SH3-containing GRB2-like protein 3-interacting protein 1 Chain: A
Molecule details ›
Chain: A
Length: 284 amino acids
Theoretical weight: 31.27 KDa
Source organism: Homo sapiens
Expression system: Enterobacteria phage L1
UniProt:
  • Canonical: Q9BQI5 (Residues: 558-828; Coverage: 33%)
Gene name: SGIP1
Sequence domains: Muniscin C-terminal mu homology domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRF BEAMLINE BL17U
Spacegroup: P21212
Unit cell:
a: 70.073Å b: 132.308Å c: 40.672Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.202 0.198 0.266
Expression system: Enterobacteria phage L1