› 6p0o

X-ray diffraction
1.54Å resolution

Crystal structure of GDP-bound human RalA

Released:
DOI: 10.2210/pdb6p0o/pdb
PDB entry 6p0o coloured by chain, front view.
PDB entry 6p0o coloured by chain, side view.
PDB entry 6p0o coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Small-molecule covalent bond formation at tyrosine creates a binding site and inhibits activation of Ral GTPases.
Bum-Erdene K, Liu D, Gonzalez-Gutierrez G, Ghozayel MK, Xu D, Meroueh SO
Proc Natl Acad Sci U S A 117 7131-7139 (2020)
PMID: 32179690

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-145721 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ras-related protein Ral-A Chain: B
Molecule details ›
Chain: B
Length: 186 amino acids
Theoretical weight: 21.3 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P11233 (Residues: 1-178; Coverage: 86%)
Gene names: RAL, RALA
Sequence domains: Ras family

Ligands and Environments

2 bound ligands:
Ligand GDP 1 x GDP
Ligand CA 1 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 4.2.2
Spacegroup: C2221
Unit cell:
a: 64.962Å b: 104.88Å c: 55.549Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.138 0.136 0.175
Expression system: Escherichia coli

Quick links

Citations

4 review citations

Inhibition of Nonfunctional Ras.
Nussinov et al. (2021)
3 more

1 mention without citation

Small-molecule covalent bond formation at tyrosine creates a binding site and inhibits activation of Ral GTPases.
Bum-Erdene et al. (2020)