› 4cq4

X-ray diffraction
1.7Å resolution

C-terminal fragment of Af1503-sol: transmembrane receptor Af1503 from Archaeoglobus fulgidus engineered for solubility

Released:
DOI: 10.2210/pdb4cq4/pdb
PDB entry 4cq4 coloured by chain, front view.
PDB entry 4cq4 coloured by chain, side view.
PDB entry 4cq4 coloured by chain, top view.
Source organism: Archaeoglobus fulgidus
Primary publication:
A soluble mutant of the transmembrane receptor Af1503 features strong changes in coiled-coil periodicity.
Hartmann MD, Dunin-Horkawicz S, Hulko M, Martin J, Coles M, Lupas AN
J Struct Biol 186 357-66 (2014)
PMID: 24568954

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-128065 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
HAMP domain-containing protein Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 309 amino acids
Theoretical weight: 34.5 KDa
Source organism: Archaeoglobus fulgidus
Expression system: Escherichia coli
UniProt:
  • Canonical: O28769 (Residues: 30-338; Coverage: 91%)
Gene name: AF_1503
Sequence domains: HAMP domain
Structure domains: hypothetical protein mp506/mpn330, domain 1

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X10SA
Spacegroup: P21
Unit cell:
a: 44.069Å b: 48.037Å c: 95.187Å
α: 90° β: 98.04° γ: 90°
R-values:
R R work R free
0.195 0.193 0.243
Expression system: Escherichia coli

Quick links

Citations

2 review citations

C-di-GMP Synthesis: Structural Aspects of Evolution, Catalysis and Regulation.
Schirmer T. (2016)
1 more

4 mentions without citation

A library of coiled-coil domains: from regular bundles to peculiar twists.
Szczepaniak et al. (2021)
3 more