› 5aws

X-ray diffraction
2Å resolution

Crystal structure of the SGIP1 mu homology domain in the P1 space group

Released:
DOI: 10.2210/pdb5aws/pdb
PDB entry 5aws coloured by chain, front view.
PDB entry 5aws coloured by chain, side view.
PDB entry 5aws coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural basis for the recognition of two consecutive mutually interacting DPF motifs by the SGIP1 μ homology domain.
Shimada A, Yamaguchi A, Kohda D
Sci Rep 6 19565 (2016)
PMID: 26822536

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-189675 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
SH3-containing GRB2-like protein 3-interacting protein 1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 282 amino acids
Theoretical weight: 30.84 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9BQI5 (Residues: 552-828; Coverage: 34%)
Gene name: SGIP1
Sequence domains: Muniscin C-terminal mu homology domain

Ligands and Environments

1 bound ligand:
Ligand ZN 12 x ZN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL32XU
Spacegroup: P1
Unit cell:
a: 37.552Å b: 53.634Å c: 75.199Å
α: 101.87° β: 86.91° γ: 95.61°
R-values:
R R work R free
0.201 0.199 0.241
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Conformational regulation of AP1 and AP2 clathrin adaptor complexes.
Beacham et al. (2019)
1 more

1 mention without citation

Structural basis for the recognition of two consecutive mutually interacting DPF motifs by the SGIP1 μ homology domain.
Shimada et al. (2016)