› 1bm5

Solution NMR

THE SOLUTION STRUCTURE OF A SITE-DIRECTED MUTANT (R111M) OF HUMAN CELLULAR RETIONIC ACID BINDING PROTEIN-TYPE II, NMR, 31 STRUCTURES

Released:
DOI: 10.2210/pdb1bm5/pdb
PDB entry 1bm5 coloured by chain, ensemble of 31 models, front view.
PDB entry 1bm5 coloured by chain, ensemble of 31 models, side view.
PDB entry 1bm5 coloured by chain, ensemble of 31 models, top view.
Source organism: Homo sapiens
Primary publication:
NMR study suggests a major role for Arg111 in maintaining the structure and dynamical properties of type II human cellular retinoic acid binding protein.
Wang L, Yan H
Biochemistry 37 13021-32 (1998)
PMID: 9737883

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-151430 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cellular retinoic acid-binding protein 2 Chain: A
Molecule details ›
Chain: A
Length: 137 amino acids
Theoretical weight: 15.56 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P29373 (Residues: 2-138; Coverage: 99%)
Gene name: CRABP2
Sequence domains: Lipocalin / cytosolic fatty-acid binding protein family
Structure domains: Lipocalin

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: DGSA
Expression system: Escherichia coli

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Citations

4 citation in other articles

The structure of Apo-wild-type cellular retinoic acid binding protein II at 1.4 A and its relationship to ligand binding and nuclear translocation.
Vaezeslami et al. (2006)
3 more