Research workbench
Crystal structure of the uba domain from cbl-B ubiquitin ligase in complex with ubiquitin
Analyse Crystal structure of the uba domain from cbl-B ubiquitin ligase 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
- 2OOB
- Type
- protein
- Length
- 116 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- E3 ubiquitin-protein ligase cbl-B; Ubiquitin
- EC
- 6.3.2.-
- UniProt
- Q13191, P62990
Structure
x-ray diffraction · 2 distinct chains · 42% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | E3 ubiquitin-protein ligase cbl-B (EC 6.3.2.-) | protein | 44 | 70% helix, 0% strand | Q13191 |
| B | Ubiquitin | protein | 72 | 25% helix, 35% strand | P62990 |
Interfaces
1 interface between chains.
- A–B · 420 Ų buried · 4 hydrogen bonds · protein-protein
Compared structures
- 2OOB · crystal structure of the UBA domain from Cbl-b ubiquitin ligase in complex with ubiquitin · the same entry in another collection · chain A against A, TM-score 1.00
- Q13191 · AlphaFold monomer V2.0 prediction for E3 ubiquitin-protein ligase cbl-B (Q13191) · a predicted model of the same protein · chain A against A, TM-score 0.91
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 Q13191
- Every structure of UniProt P62990
- Elsewhere: RCSB PDB 2OOB · PDBe 2OOB · UniProt Q13191 · UniProt P62990
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