Research workbench
Crystal structure of phosphorylated rbr E3 ligase RNF216 in complex with K63-linked di-ubiquitin
Analyse Crystal structure of phosphorylated rbr E3 ligase RNF216 in complex with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7M4O
- Type
- protein
- Length
- 268 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q9NWF9, P0CG48
- Ligands
- ZN, SO4
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 116 | — | Q9NWF9 |
| B, C | — | protein | 76 | — | P0CG48 |
Ligands and binding sites
- ZN · Zinc ion · metal · 3 copies · chains A
- SO4 · Sulfate ion · ion · 3 copies · chains A, B, C
- GOL · Glycerol · additive · 3 copies · chains A, B
- PG0 · 2-(2-methoxyethoxy)ethanol · additive · chains A, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 7M4O · Crystal structure of phosphorylated RBR E3 ligase RNF216 in complex with K63-linked… · the same entry in another collection · chain A against A, TM-score 1.00
- Q9NWF9 · AlphaFold monomer V2.0 prediction for E3 ubiquitin-protein ligase RNF216 (Q9NWF9) · a predicted model of the same protein · chain A against A, TM-score 0.83
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 Q9NWF9
- Every structure of UniProt P0CG48
- Elsewhere: RCSB PDB 7M4O · PDBe 7M4O · UniProt Q9NWF9 · UniProt P0CG48
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