› 2fmr

Solution NMR

KH1 FROM THE FRAGILE X PROTEIN FMR1, NMR, 18 STRUCTURES

Released:
DOI: 10.2210/pdb2fmr/pdb
PDB entry 2fmr coloured by chain, ensemble of 18 models, front view.
PDB entry 2fmr coloured by chain, ensemble of 18 models, side view.
PDB entry 2fmr coloured by chain, ensemble of 18 models, top view.
Source organism: Homo sapiens
Primary publication:
The solution structure of the first KH domain of FMR1, the protein responsible for the fragile X syndrome.
Musco G, Kharrat A, Stier G, Fraternali F, Gibson TJ, Nilges M, Pastore A
Nat Struct Biol 4 712-6 (1997)
PMID: 9302998

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Fragile X messenger ribonucleoprotein 1 Chain: A
Molecule details ›
Chain: A
Length: 65 amino acids
Theoretical weight: 7.27 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q06787 (Residues: 216-280; Coverage: 10%)
Gene name: FMR1
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
Refinement method: simulated annealing
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

13 review citations

Exoribonuclease superfamilies: structural analysis and phylogenetic distribution.
Zuo et al. (2001)
12 more

3 mentions without citation

Refinement of homology-based protein structures by molecular dynamics simulation techniques.
Fan et al. (2004)
2 more