› 5awr

X-ray diffraction
2.5Å resolution

Crystal structure of the SGIP1 mu homology domain in the P4212 space group

Released:
DOI: 10.2210/pdb5awr/pdb
PDB entry 5awr coloured by chain, front view.
PDB entry 5awr coloured by chain, side view.
PDB entry 5awr 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 Chain: A
Molecule details ›
Chain: A
Length: 282 amino acids
Theoretical weight: 31.13 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 4 x ZN
1 modified residue:
Ligand MSE 6 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL26B1
Spacegroup: P4212
Unit cell:
a: 109.826Å b: 109.826Å c: 79.492Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.201 0.199 0.247
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)