› 1kqw

X-ray diffraction
1.38Å resolution

Crystal structure of holo-CRBP from zebrafish

Released:
DOI: 10.2210/pdb1kqw/pdb
PDB entry 1kqw coloured by chain, front view.
PDB entry 1kqw coloured by chain, side view.
PDB entry 1kqw coloured by chain, top view.
Source organism: Danio rerio
Primary publication:
Identification and structural analysis of a zebrafish apo and holo cellular retinol-binding protein.
Calderone V, Folli C, Marchesani A, Berni R, Zanotti G
J Mol Biol 321 527-35 (2002)
PMID: 12162964

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-186528 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cytosolic fatty-acid binding proteins domain-containing protein Chain: A
Molecule details ›
Chain: A
Length: 134 amino acids
Theoretical weight: 15.7 KDa
Source organism: Danio rerio
Expression system: Escherichia coli
UniProt:
  • Canonical: Q8UVG6 (Residues: 2-135; Coverage: 99%)
Gene names: CRBP, CRBPII, rbp2, rbp2a, wu:fb69e02
Sequence domains: Lipocalin / cytosolic fatty-acid binding protein family
Structure domains: Lipocalin

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-4
Spacegroup: I4
Unit cell:
a: 89.018Å b: 89.018Å c: 38.271Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.165 0.159 0.233
Expression system: Escherichia coli

Quick links

Citations

9 citation in other articles

The role of flexibility and conformational selection in the binding promiscuity of PDZ domains.
Münz et al. (2012)
8 more

5 mentions without citation

Recognition of functional sites in protein structures.
Shulman-Peleg et al. (2004)
4 more