› 5k8q

X-ray diffraction
1.74Å resolution

Crystal Structure of Calcium-loaded Calmodulin in complex with STRA6 CaMBP2-site peptide.

Released:
DOI: 10.2210/pdb5k8q/pdb
PDB entry 5k8q coloured by chain, front view.
PDB entry 5k8q coloured by chain, side view.
PDB entry 5k8q coloured by chain, top view.
Source organisms:
Primary publication:
Structure of the STRA6 receptor for retinol uptake.
Chen Y, Clarke OB, Kim J, Stowe S, Kim YK, Assur Z, Cavalier M, Godoy-Ruiz R, von Alpen DC, Manzini C, Blaner WS, Frank J, Quadro L, Weber DJ, Shapiro L, Hendrickson WA, Mancia F
Science 353 (2016)
PMID: 27563101

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-123353 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Calmodulin-1 Chain: A
Molecule details ›
Chain: A
Length: 149 amino acids
Theoretical weight: 16.85 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P0DP23 (Residues: 1-149; Coverage: 100%)
Gene names: CALM, CALM1, CAM, CAM1
Sequence domains: EF-hand domain pair
Receptor for retinol uptake stra6 Chain: B
Molecule details ›
Chain: B
Length: 29 amino acids
Theoretical weight: 3.08 KDa
Source organism: Danio rerio
Expression system: Not provided
UniProt:
  • Canonical: F1RAX4 (Residues: 600-626; Coverage: 4%)
Gene name: stra6

Ligands and Environments

2 bound ligands:
Ligand CA 4 x CA
Ligand IMD 1 x IMD
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-E
Spacegroup: C2
Unit cell:
a: 156.51Å b: 37.23Å c: 35.73Å
α: 90° β: 94.35° γ: 90°
R-values:
R R work R free
0.229 0.227 0.267
Expression systems:
  • Escherichia coli BL21(DE3)
  • Not provided

Quick links

Citations

25 review citations

Biochemical and physiological importance of the CYP26 retinoic acid hydroxylases.
Isoherranen et al. (2019)
24 more

5 mentions without citation

Binding and Functional Folding (BFF): A Physiological Framework for Studying Biomolecular Interactions and Allostery.
Young et al. (2022)
4 more