MolNFT v2 · #73498 · protein
A Dual E3 Mechanism for Rub1 Ligation to Cdc53: Dcn1(P)-Cdc53(WHB)
3O2P: “A Dual E3 Mechanism for Rub1 Ligation to Cdc53: Dcn1(P)-Cdc53(WHB)”. X-ray diffraction at 2.233. MolNFT v2 #73498 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 3O2P
- Type
- protein
- Length
- 285 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.233
- Source
- Saccharomyces cerevisiae
- UniProt
- Q12395, Q12018
Structure
x-ray diffraction · resolution 2.233 · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 199 | — | Q12395 |
| E | — | protein | 86 | — | Q12018 |
Compared structures
- 3O2P · A dual E3 mechanism for RUB1 ligation to CDC53: DCN1(P)-CDC53(WHB) · the same entry in another collection · chain A against A, TM-score 1.00
- Q12395 · AlphaFold monomer V2.0 prediction for defective in cullin neddylation protein 1 (Q12395) · a predicted model of the same protein · chain A against A, TM-score 0.99
- Q12018 · AlphaFold monomer V2.0 prediction for cell division control protein 53 (Q12018) · a predicted model of the same protein · chain E against A, TM-score 0.92
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 Q12395
- Every structure of UniProt Q12018
- Elsewhere: RCSB PDB 3O2P · PDBe 3O2P · UniProt Q12395 · UniProt Q12018
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