› 3ryt

X-ray diffraction
3.58Å resolution

The Plexin A1 intracellular region in complex with Rac1

Released:
DOI: 10.2210/pdb3ryt/pdb
PDB entry 3ryt coloured by chain, front view.
PDB entry 3ryt coloured by chain, side view.
PDB entry 3ryt coloured by chain, top view.
Source organisms:
Primary publication:
Plexins are GTPase-activating proteins for Rap and are activated by induced dimerization.
Wang Y, He H, Srivastava N, Vikarunnessa S, Chen YB, Jiang J, Cowan CW, Zhang X
Sci Signal 5 ra6 (2012)
PMID: 22253263

Function and Biology Details

Reaction catalysed: 
GTP + H(2)O = GDP + phosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assemblies composition:
hetero dimer (preferred)
monomeric
Assembly name:
PDBe Complex ID:
PDB-CPX-158896 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Plexin-A1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 626 amino acids
Theoretical weight: 71.88 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
UniProt:
  • Canonical: P70206 (Residues: 1269-1894; Coverage: 34%)
Gene names: Kiaa4053, Plxna1
Sequence domains:
Structure domains:
Ras-related C3 botulinum toxin substrate 1 Chain: C
Molecule details ›
Chain: C
Length: 180 amino acids
Theoretical weight: 19.99 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P63000 (Residues: 1-177; Coverage: 92%)
Gene names: MIG5, RAC1, TC25
Sequence domains: Ras family
Structure domains: P-loop containing nucleotide triphosphate hydrolases

Ligands and Environments

2 bound ligands:
Ligand MG 1 x MG
Ligand GNP 1 x GNP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: P43212
Unit cell:
a: 110.783Å b: 110.783Å c: 265.628Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.274 0.27 0.34
Expression systems:
  • Escherichia coli
  • Escherichia coli BL21(DE3)

Quick links

Citations

36 review citations

Semaphorins and plexins as therapeutic targets.
Worzfeld et al. (2014)
35 more

6 mentions without citation

Structural mechanisms of plexin signaling.
Pascoe et al. (2015)
5 more