› 2ggz

X-ray diffraction
3Å resolution

Crystal Structure of Human Guanylate Cyclase Activating Protein-3

Released:
DOI: 10.2210/pdb2ggz/pdb
PDB entry 2ggz coloured by chain, front view.
PDB entry 2ggz coloured by chain, side view.
PDB entry 2ggz coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
The crystal structure of GCAP3 suggests molecular mechanism of GCAP-linked cone dystrophies.
Stephen R, Palczewski K, Sousa MC
J Mol Biol 359 266-75 (2006)
PMID: 16626734

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-132069 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Guanylyl cyclase-activating protein 3 Chains: A, B
Molecule details ›
Chains: A, B
Length: 211 amino acids
Theoretical weight: 24.04 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: O95843 (Residues: 1-209; Coverage: 100%)
Gene names: GCAP3, GUCA1C
Sequence domains: EF hand
Structure domains: EF-hand

Ligands and Environments

1 bound ligand:
Ligand CA 6 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 5.0.3, ALS BEAMLINE 8.2.1
Spacegroup: P43
Unit cell:
a: 88.19Å b: 88.19Å c: 71.02Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.256 0.256 0.29
Expression system: Escherichia coli BL21

Quick links

Citations

9 review citations

Neuronal calcium sensor proteins: generating diversity in neuronal Ca2+ signalling.
Burgoyne RD. (2007)
8 more

2 mentions without citation

Molecular Properties of Human Guanylate Cyclase-Activating Protein 3 (GCAP3) and Its Possible Association with Retinitis Pigmentosa.
Avesani et al. (2022)
1 more