› 7aa1

X-ray diffraction
1.71Å resolution

Structural comparison of cellular retinoic acid binding proteins I and II in the presence and absence of natural and synthetic ligands

Released:
DOI: 10.2210/pdb7aa1/pdb
PDB entry 7aa1 coloured by chain, front view.
PDB entry 7aa1 coloured by chain, side view.
PDB entry 7aa1 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structure-functional relationship of cellular retinoic acid-binding proteins I and II interacting with natural and synthetic ligands.
Tomlinson CWE, Cornish KAS, Whiting A, Pohl E
Acta Crystallogr D Struct Biol 77 164-175 (2021)
PMID: 33559606

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-151430 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cellular retinoic acid-binding protein 2 Chain: AAA
Molecule details ›
Chain: AAA
Length: 138 amino acids
Theoretical weight: 15.71 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P29373 (Residues: 1-138; Coverage: 100%)
Gene name: CRABP2
Sequence domains: Lipocalin / cytosolic fatty-acid binding protein family

Ligands and Environments

1 bound ligand:
Ligand R62 1 x R62
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I24
Spacegroup: P213
Unit cell:
a: 78.56Å b: 78.56Å c: 78.56Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.181 0.18 0.201
Expression system: Escherichia coli

Quick links

Citations

1 review citation

CRABP1 in Non-Canonical Activities of Retinoic Acid in Health and Diseases.
Nhieu et al. (2022)
2 other articles

1 mention without citation

Structure-functional relationship of cellular retinoic acid-binding proteins I and II interacting with natural and synthetic ligands.
Tomlinson et al. (2021)