› 1nty

X-ray diffraction
1.7Å resolution

Crystal structure of the first DH/PH domain of Trio to 1.7 A

Released:
DOI: 10.2210/pdb1nty/pdb
PDB entry 1nty coloured by chain, front view.
PDB entry 1nty coloured by chain, side view.
PDB entry 1nty coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
The C-terminal basic tail of RhoG assists the guanine nucleotide exchange factor trio in binding to phospholipids.
Skowronek KR, Guo F, Zheng Y, Nassar N
J Biol Chem 279 37895-907 (2004)
PMID: 15199069

Function and Biology Details

Reaction catalysed: 
ATP + a protein = ADP + a phosphoprotein
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-131183 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Triple functional domain protein Chain: A
Molecule details ›
Chain: A
Length: 311 amino acids
Theoretical weight: 36.43 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: O75962 (Residues: 1284-1594; Coverage: 10%)
Gene name: TRIO
Sequence domains:
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: CHESS BEAMLINE A1
Spacegroup: P3121
Unit cell:
a: 99.54Å b: 99.54Å c: 98.294Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.195 0.195 0.214
Expression system: Escherichia coli BL21

Quick links

Citations

7 review citations

GEF means go: turning on RHO GTPases with guanine nucleotide-exchange factors.
Rossman et al. (2005)
6 more

16 mentions without citation

Protein-protein docking benchmark version 3.0.
Hwang et al. (2008)
15 more