Research workbench
Solution structure of ubiquitin-like domain of HHR23B complexed with ubiquitin-interacting motif of proteasome subunit S5A
Analyse Solution structure of ubiquitin-like domain of HHR23B complexed with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1UEL
- Type
- protein
- Length
- 143 residues
- Chains
- 2
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- UV excision repair protein RAD23 homolog B; 26S proteasome non-ATPase regulatory subunit 4
- UniProt
- P54727, P55036
- Pockets
- 1 · best druggability 0.48
Structure
solution nmr · 2 distinct chains · 24% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | UV excision repair protein RAD23 homolog B | protein | 95 | 21% helix, 27% strand | P54727 |
| B | 26S proteasome non-ATPase regulatory subunit 4 | protein | 48 | 31% helix, 0% strand | P55036 |
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 94 | 0.48 | 0.81 | 20 | empty |
Interfaces
1 interface between chains.
- A–B · 756 Ų buried · 10 hydrogen bonds · protein-protein
Compared structures
- 1UEL · Solution structure of ubiquitin-like domain of hHR23B complexed with… · the same entry in another collection · chain A against A, TM-score 1.00
- P54727 · AlphaFold monomer V2.0 prediction for UV excision repair protein RAD23 homolog B (P54727) · a predicted model of the same protein · chain A against A, TM-score 0.76
- P55036 · AlphaFold monomer V2.0 prediction for 26S proteasome non-ATPase regulatory subunit 4… · a predicted model of the same protein · chain B against A, TM-score 0.42
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 P54727
- Every structure of UniProt P55036
- Elsewhere: RCSB PDB 1UEL · PDBe 1UEL · UniProt P54727 · UniProt P55036
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