› 1koh

X-ray diffraction
3.8Å resolution

THE CRYSTAL STRUCTURE AND MUTATIONAL ANALYSIS OF A NOVEL RNA-BINDING DOMAIN FOUND IN THE HUMAN TAP NUCLEAR MRNA EXPORT FACTOR

Released:
DOI: 10.2210/pdb1koh/pdb
PDB entry 1koh coloured by chain, front view.
PDB entry 1koh coloured by chain, side view.
PDB entry 1koh coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
The crystal structure and mutational analysis of a novel RNA-binding domain found in the human Tap nuclear mRNA export factor.
Ho DN, Coburn GA, Kang Y, Cullen BR, Georgiadis MM
Proc Natl Acad Sci U S A 99 1888-93 (2002)
PMID: 11854490

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-193679 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Nuclear RNA export factor 1 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 277 amino acids
Theoretical weight: 31.48 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9UBU9 (Residues: 96-372; Coverage: 45%)
Gene names: NXF1, TAP
Sequence domains: Tap, RNA-binding
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X25
Spacegroup: P41212
Unit cell:
a: 136.779Å b: 136.779Å c: 202.922Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.275 0.275 0.355
Expression system: Escherichia coli BL21(DE3)

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Citations

15 citation in other articles

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4 mentions without citation

Amino acid residue doublet propensity in the protein-RNA interface and its application to RNA interface prediction.
Kim et al. (2006)
3 more