› 6k1z

X-ray diffraction
2.31Å resolution

Crystal structure of farnesylated hGBP1

Released:
DOI: 10.2210/pdb6k1z/pdb
PDB entry 6k1z coloured by chain, front view.
PDB entry 6k1z coloured by chain, side view.
PDB entry 6k1z coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural mechanism for guanylate-binding proteins (GBPs) targeting by the Shigella E3 ligase IpaH9.8.
Ji C, Du S, Li P, Zhu Q, Yang X, Long C, Yu J, Shao F, Xiao J
PLoS Pathog 15 e1007876 (2019)
PMID: 31216343

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-152319 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Guanylate-binding protein 1 Chain: A
Molecule details ›
Chain: A
Length: 594 amino acids
Theoretical weight: 68.17 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P32455 (Residues: 1-592; Coverage: 100%)
Gene name: GBP1
Sequence domains:

Ligands and Environments

1 bound ligand:
Ligand FAR 1 x FAR
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRF BEAMLINE BL17U1
Spacegroup: P212121
Unit cell:
a: 48.184Å b: 113.959Å c: 127.475Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.223 0.22 0.267
Expression system: Escherichia coli

Quick links

Citations

6 review citations

The T3SS of Shigella: Expression, Structure, Function, and Role in Vacuole Escape.
Bajunaid et al. (2020)
5 more

7 mentions without citation

Human guanylate binding proteins: nanomachines orchestrating host defense.
Kutsch et al. (2021)
6 more