Research workbench
HHR23A protein structure based on residual dipolar coupling data
Analyse HHR23A protein structure based on residual dipolar coupling data in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1QZE
- Type
- protein
- Length
- 214 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P54725
Structure
solution nmr · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 214 | — | P54725 |
Compared structures
- 1QZE · HHR23a protein structure based on residual dipolar coupling data · 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 0.34
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 1QZE · PDBe 1QZE · UniProt P54725
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