Research workbench
Solution structure of the RAD23 ubiquitin-like (ubl) domain
Analyse Solution structure of the RAD23 ubiquitin-like (ubl) domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2NBU
- Type
- protein
- Length
- 78 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- UV excision repair protein RAD23
- UniProt
- P32628
Structure
solution nmr · 1 distinct chain · 21% helix, 31% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | UV excision repair protein RAD23 | protein | 78 | 21% helix, 31% strand | P32628 |
Compared structures
- 2NBU · Solution structure of the Rad23 ubiquitin-like (UBL) domain · the same entry in another collection · chain A against A, TM-score 1.00
- P32628 · AlphaFold monomer V2.0 prediction for UV excision repair protein RAD23 (P32628) · a predicted model of the same protein · chain A against A, TM-score 0.94
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 P32628
- Elsewhere: RCSB PDB 2NBU · PDBe 2NBU · UniProt P32628
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