› 1fut

X-ray diffraction
2Å resolution

CRYSTAL STRUCTURES OF RIBONUCLEASE F1 OF FUSARIUM MONILIFORME IN ITS FREE FORM AND IN COMPLEX WITH 2'GMP

Released:
DOI: 10.2210/pdb1fut/pdb
PDB entry 1fut coloured by chain, front view.
PDB entry 1fut coloured by chain, side view.
PDB entry 1fut coloured by chain, top view.
Source organism: Fusarium fujikuroi
Primary publication:
Crystal structures of ribonuclease F1 of Fusarium moniliforme in its free form and in complex with 2'GMP.
Vassylyev DG, Katayanagi K, Ishikawa K, Tsujimoto-Hirano M, Danno M, Pähler A, Matsumoto O, Matsushima M, Yoshida H, Morikawa K
J Mol Biol 230 979-96 (1993)
PMID: 8386773

Function and Biology Details

Reaction catalysed: 
(1a) (RNA) containing guanosine = (RNA fragment)-3'-guanosine-2',3'-cyclophosphate + a 5'-hydroxy-ribonucleotide-3'-(RNA fragment)
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-145261 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Guanyl-specific ribonuclease F1 Chain: A
Molecule details ›
Chain: A
Length: 106 amino acids
Theoretical weight: 10.99 KDa
Source organism: Fusarium fujikuroi
Expression system: Not provided
UniProt:
  • Canonical: P10282 (Residues: 26-131; Coverage: 100%)
Structure domains: Microbial ribonucleases

Ligands and Environments

1 bound ligand:
Ligand 2GP 1 x 2GP
1 modified residue:
Ligand PCA 1 x PCA

Experiments and Validation Details

Entry percentile scores
Spacegroup: P61
Unit cell:
a: 40.16Å b: 40.16Å c: 120.85Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.168 not available not available
Expression system: Not provided

Quick links

Citations

13 citation in other articles

Asparagine and glutamine: using hydrogen atom contacts in the choice of side-chain amide orientation.
Word et al. (1999)
12 more

3 mentions without citation

Protein pockets: inventory, shape, and comparison.
Coleman et al. (2010)
2 more