› 1dt4

X-ray diffraction
2.6Å resolution

CRYSTAL STRUCTURE OF NOVA-1 KH3 K-HOMOLOGY RNA-BINDING DOMAIN

Released:
DOI: 10.2210/pdb1dt4/pdb
PDB entry 1dt4 coloured by chain, front view.
PDB entry 1dt4 coloured by chain, side view.
PDB entry 1dt4 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Crystal structures of Nova-1 and Nova-2 K-homology RNA-binding domains.
Lewis HA, Chen H, Edo C, Buckanovich RJ, Yang YY, Musunuru K, Zhong R, Darnell RB, Burley SK
Structure 7 191-203 (1999)
PMID: 10368286

Function and Biology Details

Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-156345 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
RNA-binding protein Nova-1 Chain: A
Molecule details ›
Chain: A
Length: 73 amino acids
Theoretical weight: 7.9 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P51513 (Residues: 421-492; Coverage: 14%)
Gene name: NOVA1
Sequence domains: KH domain
Structure domains: K Homology domain, type 1

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: P42212
Unit cell:
a: 44.67Å b: 44.67Å c: 84.02Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.242 0.222 0.282
Expression system: Escherichia coli

Quick links

Citations

15 review citations

The poly(C)-binding proteins: a multiplicity of functions and a search for mechanisms.
Makeyev et al. (2002)
14 more

4 mentions without citation

Thermodynamic propensities of amino acids in the native state ensemble: implications for fold recognition.
Wrabl et al. (2001)
3 more