› 4rj9

X-ray diffraction
1.63Å resolution

Function and Biology Details

Reaction catalysed: 
(1a) ATP + [DNA ligase]-L-lysine = [DNA ligase]-N(6)-(5'-adenylyl)-L-lysine + diphosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-180566 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
GTPase activating protein 1 Chain: A
Molecule details ›
Chain: A
Length: 165 amino acids
Theoretical weight: 18.57 KDa
Source organism: Oryza sativa Japonica Group
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q6YWF1 (Residues: 1-165; Coverage: 100%)
Gene names: GAP1, GPBP1, LOC_Os02g22130, OSJNBb0042G06.10, Os02g0327000, OsJ_06508, P0476C12.36
Sequence domains: C2 domain

Ligands and Environments

1 bound ligand:
Ligand K 2 x K
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU FR-E SUPERBRIGHT
Spacegroup: C2221
Unit cell:
a: 37.19Å b: 166.75Å c: 60.73Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.185 0.183 0.204
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

2 review citations

Structural comparison of unconventional G protein YchF with heterotrimeric G protein and small G protein.
Luo et al. (2022)
1 more

2 mentions without citation

The Universally Conserved Unconventional G Protein YchF Is Critical for Growth and Stress Response.
Lin et al. (2023)
1 more