Research workbench

Regnase-1 zinc finger domain

Analyse Regnase-1 zinc finger domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2N5K
Type: protein
Length: 29 residues
Chains: 1
Method: solution nmr
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Ribonuclease ZC3H12A
EC: 3.1.-.-
UniProt: Q5D1E7
Ligands: ZN

Structure

solution nmr · 1 distinct chain · 0% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Ribonuclease ZC3H12A (EC 3.1.-.-)	protein	29	0% helix, 0% strand	Q5D1E7

Ligands and binding sites

ZN · Zinc ion · metal · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Compared structures

2N5K · Regnase-1 Zinc finger domain · the same entry in another collection · chain A against A, TM-score 1.00
Q5D1E7 · AlphaFold monomer V2.0 prediction for endoribonuclease ZC3H12A (Q5D1E7) · a predicted model of the same protein · chain A against A, TM-score 0.48

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt Q5D1E7
Elsewhere: RCSB PDB 2N5K · PDBe 2N5K · UniProt Q5D1E7

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.