MolNFT v2 · #116947 · protein
A C2HC zinc finger is essential for the activity of the RING ubiquitin ligase RNF125
5DKA: “A C2HC zinc finger is essential for the activity of the RING ubiquitin ligase RNF125”. X-ray diffraction at 1.55, 3 ligands (ZN, MG, CL). MolNFT v2 #116947 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 5DKA
- Type
- protein
- Length
- 192 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.55
- Source
- Homo sapiens
- UniProt
- Q96EQ8
- Ligands
- ZN, MG, CL
Structure
x-ray diffraction · resolution 1.55 · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | — | protein | 96 | — | Q96EQ8 |
Ligands and binding sites
- ZN · Zinc ion · metal · 6 copies · chains A, B
- MG · Magnesium ion · metal · chains B
- CL · Chloride ion · ion · 4 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 5DKA · A C2HC zinc finger is essential for the activity of the ring ubiquitin ligase RNF125 · the same entry in another collection · chain A against A, TM-score 1.00
- Q96EQ8 · AlphaFold monomer V2.0 prediction for E3 ubiquitin-protein ligase RNF125 (Q96EQ8) · a predicted model of the same protein · chain A against A, TM-score 0.95
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 Q96EQ8
- Elsewhere: RCSB PDB 5DKA · PDBe 5DKA · UniProt Q96EQ8
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