› 1sgl

X-ray diffraction
2.2Å resolution

The three-dimensional structure and X-ray sequence reveal that trichomaglin is a novel S-like ribonuclease

Released:
DOI: 10.2210/pdb1sgl/pdb
PDB entry 1sgl coloured by chain, front view.
PDB entry 1sgl coloured by chain, side view.
PDB entry 1sgl coloured by chain, top view.
Source organism: Trichosanthes lepiniana
Primary publication:
The three-dimensional structure and X-ray sequence reveal that trichomaglin is a novel S-like ribonuclease.
Gan JH, Yu L, Wu J, Xu H, Choudhary JS, Blackstock WP, Liu WY, Xia ZX
Structure 12 1015-25 (2004)
PMID: 15274921

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-122667 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Trichomaglin Chain: A
Molecule details ›
Chain: A
Length: 209 amino acids
Theoretical weight: 23.55 KDa
Source organism: Trichosanthes lepiniana
UniProt:
  • Canonical: E0CX00 (Residues: 1-209; Coverage: 100%)
Sequence domains: Ribonuclease T2 family
Structure domains: Ribonuclease T2-like

Ligands and Environments

1 bound ligand:
Ligand SO4 4 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P61
Unit cell:
a: 93.99Å b: 93.99Å c: 57.765Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.203 0.199 0.237

Quick links

Citations

3 citation in other articles

RNase T2 genes from rice and the evolution of secretory ribonucleases in plants.
MacIntosh et al. (2010)
2 more