Research workbench
Complex of RAD18 (RAD6 binding domain) with RAD6B
Analyse Complex of RAD18 (RAD6 binding domain) with RAD6B in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2YBF
- Type
- protein
- Length
- 171 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ubiquitin-conjugating enzyme E2 B; E3 ubiquitin-protein ligase RAD18
- EC
- 6.3.2.19, 6.3.2.-
- UniProt
- P63146, Q9NS91
- Ligands
- NA, SO4
Structure
x-ray diffraction · 2 distinct chains · 40% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ubiquitin-conjugating enzyme E2 B (EC 6.3.2.19) | protein | 150 | 35% helix, 20% strand | P63146 |
| B | E3 ubiquitin-protein ligase RAD18 (EC 6.3.2.-) | protein | 21 | 76% helix, 0% strand | Q9NS91 |
Ligands and binding sites
- NA · Sodium ion · metal · chains A
- SO4 · Sulfate ion · ion · 2 copies · chains A, B
- BME · Beta-mercaptoethanol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- A–B · 914 Ų buried · 15 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 covalent (additive adduct).
Compared structures
- 2YBF · Complex of Rad18 (Rad6 binding domain) with Rad6b · the same entry in another collection · chain A against A, TM-score 1.00
- P63146 · AlphaFold monomer V2.0 prediction for ubiquitin-conjugating enzyme E2 B (P63146) · a predicted model of the same protein · chain A against A, TM-score 0.99
- Q9NS91 · AlphaFold monomer V2.0 prediction for E3 ubiquitin-protein ligase RAD18 (Q9NS91) · a predicted model of the same protein · chain B against A, TM-score 0.53
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 P63146
- Every structure of UniProt Q9NS91
- Elsewhere: RCSB PDB 2YBF · PDBe 2YBF · UniProt P63146 · UniProt Q9NS91
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