Research workbench
The crystal structure of the ubiquitin-like (ubl) domain of HHR23A (human homologue a of RAD23)
Analyse The crystal structure of the ubiquitin-like (ubl) domain of HHR23A (human… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2WYQ
- Type
- protein
- Length
- 77 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- UV excision repair protein RAD23 homolog a
- UniProt
- P54725
- Ligands
- SO4
Structure
x-ray diffraction · 1 distinct chain · 25% helix, 36% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | UV excision repair protein RAD23 homolog a | protein | 77 | 25% helix, 36% strand | P54725 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 2WYQ · The crystal structure of the ubiquitin-like (ubl) domain of HHR23A (human homologue a of… · the same entry in another collection · chain A against A, TM-score 1.00
- P54725 · AlphaFold monomer V2.0 prediction for UV excision repair protein RAD23 homolog a (P54725) · a predicted model of the same protein · chain A against A, TM-score 0.97
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 P54725
- Elsewhere: RCSB PDB 2WYQ · PDBe 2WYQ · UniProt P54725
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