Crystal structure of the RNF4 ring domain dimer. Determined by X-ray diffraction at 1.8 Å resolution. Released 6 Oct 2010.
Explore 3NG2 in 3D Show helices and sheets RCSB PDB PDBe
3NG2 contains 4 α-helices and 12 β-strands across 2 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 135 | 1 | 1 |
| β-strand | 142 | 1 | 1 |
| α-helix | 143-147 | 5 | |
| β-strand | 153-155 | 3 | 2 |
| β-strand | 161-163 | 3 | 2 |
| α-helix | 164-173 | 10 | |
| β-strand | 176 | 1 | 3 |
| β-strand | 183 | 1 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 135 | 1 | 4 |
| β-strand | 142 | 1 | 4 |
| α-helix | 143-148 | 6 | |
| β-strand | 153-155 | 3 | 5 |
| β-strand | 161-163 | 3 | 5 |
| α-helix | 164-171 | 8 | |
| β-strand | 176 | 1 | 6 |
| β-strand | 183 | 1 | 6 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| RING finger protein 4 | A, B | protein | 71 | Rattus norvegicus | O88846 (AlphaFold model) |
>3NG2_1 RING finger protein 4 (chains A, B) GTTGLRPSGTVSCPICMDGYSEIVQNGRLIVSTECGHVFCSQCLRDSLKNANTCPTCRKK INHKRYHPIYI
| ID | Name | Formula | Copies |
|---|---|---|---|
| ZN | Zinc ion | Zn | 4 |
Water and common crystallization additives (SO4) are not listed.
RING domain dimerization is essential for RNF4 function. Liew, C.W., Sun, H., Hunter, T. et al. Biochem J (2010) 431:23-29. DOI 10.1042/BJ20100957 · PubMed
Other PDB entries of the same protein (UniProt O88846 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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