3LJD: The X-ray structure of zebrafish RNase1 from a new crystal form at pH 4.5

Recently, extracellular RNases of the RNase A superfamily, with the characteristic CKxxNTF sequence signature, have been identified in fish. This has led to the recognition that these RNases are present in the whole vertebrate subphylum. In fact, they comprise the only enzyme family unique to vertebrates. Four RNases from zebrafish (Danio rerio) have been previously reported and have a very low RNase activity; some of these are endowed, like human angiogenin, with powerful angiogenic and bactericidal activities. In the present paper, we report the three-dimensional structure, the thermodynamic behaviour and the biological properties of a novel zebrafish RNase, ZF-RNase-5. The investigation of its structural and functional properties, extended to all other subfamily members, provides an inclusive description of the whole zebrafish RNase subfamily.
PDB ID: 3LJDDownload
MMDB ID: 87151
PDB Deposition Date: 2010/1/26
Updated in MMDB: 2010/12
Experimental Method:
x-ray diffraction
Resolution: 1.38  Å
Source Organism:
Similar Structures:
Biological Unit for 3LJD: monomeric; determined by author
Molecular Components in 3LJD
Label Count Molecule
Protein (1 molecule)
Zebrafish Rnase1
Molecule annotation
Chemicals (4 molecules)
* Click molecule labels to explore molecular sequence information.

Citing MMDB