Research workbench
Solution structure of the alpha-crystallin domain from the redox- sensitive chaperone, HSPB1
Analyse Solution structure of the alpha-crystallin domain from the redox- sensitive… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2N3J
- Type
- protein
- Length
- 196 residues
- Chains
- 2
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P04792
Structure
solution nmr · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | — | protein | 98 | — | P04792 |
Compared structures
- 2N3J · Solution Structure of the alpha-crystallin domain from the redox-sensitive chaperone… · the same entry in another collection · chain A against A, TM-score 1.00
- P04792 · AlphaFold monomer V2.0 prediction for heat shock protein beta-1 (P04792) · a predicted model of the same protein · chain A against A, TM-score 0.63
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 P04792
- Elsewhere: RCSB PDB 2N3J · PDBe 2N3J · UniProt P04792
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