1wh9

Solution NMR

Solution structure of the KH domain of human ribosomal protein S3

Released:
Source organism: Homo sapiens
Entry authors: Nameki N, Tomizawa T, Koshiba S, Kigawa T, Yokoyama S, RIKEN Structural Genomics/Proteomics Initiative (RSGI)

Function and Biology Details

Reaction catalysed:
The C-O-P bond 3' to the apurinic or apyrimidinic site in DNA is broken by a beta-elimination reaction, leaving a 3'-terminal unsaturated sugar and a product with a terminal 5'-phosphate
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-149952 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Small ribosomal subunit protein uS3 Chain: A
Molecule details ›
Chain: A
Length: 92 amino acids
Theoretical weight: 9.92 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P23396 (Residues: 17-95; Coverage: 33%)
Gene names: OK/SW-cl.26, RPS3
Sequence domains: KH domain
Structure domains: GMP Synthetase; Chain A, domain 3

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: torsion angle dynamics, restrained molecular dynamics
Expression system: Not provided