› 7p8p

X-ray diffraction
2.34Å resolution

Crystal structure of Fhit covalently bound to a nucleotide

Released:
DOI: 10.2210/pdb7p8p/pdb
PDB entry 7p8p coloured by chain, front view.
PDB entry 7p8p coloured by chain, side view.
PDB entry 7p8p coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Chemical Proteomics of the Tumor Suppressor Fhit Covalently Bound to the Cofactor Ap3A Elucidates Its Inhibitory Action on Translation.
Herzog D, Jansen J, Mißun M, Diederichs K, Stengel F, Marx A
OpenAccess logo J Am Chem Soc 144 8613-8623 (2022)
PMID: 35522782

Function and Biology Details

Reactions catalysed: 
Adenylyl sulfate + NH(3) = adenosine 5'-phosphoramidate + sulfate
P(1)-P(3)-bis(5'-adenosyl) triphosphate + H(2)O = ADP + AMP
Adenylyl sulfate + H(2)O = AMP + sulfate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-156029 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Bis(5'-adenosyl)-triphosphatase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 163 amino acids
Theoretical weight: 18.8 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P49789 (Residues: 1-147; Coverage: 100%)
Gene name: FHIT
Sequence domains: HIT domain

Ligands and Environments

3 bound ligands:
Ligand 6BI 4 x 6BI
Ligand NA 3 x NA
Ligand TRS 1 x TRS
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06DA
Spacegroup: P212121
Unit cell:
a: 52.422Å b: 61.736Å c: 198.009Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.197 0.193 0.246
Expression system: Escherichia coli

Quick links

Citations

3 citation in other articles

The Alarmone Diadenosine Tetraphosphate as a Cosubstrate for Protein AMPylation.
Frese et al. (2023)
2 more

1 mention without citation

Chemical Proteomics of the Tumor Suppressor Fhit Covalently Bound to the Cofactor Ap3A Elucidates Its Inhibitory Action on Translation.
Herzog et al. (2022)