Research workbench
NMR structure of HSP12, a protein induced by and required for dietary restriction-induced lifespan extension in yeast.
Analyse NMR structure of HSP12, a protein induced by and required for dietary… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4AXP
- Type
- protein
- Length
- 109 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 12 kda heat shock protein
- UniProt
- P22943
Structure
solution nmr · 1 distinct chain · 63% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 12 kda heat shock protein | protein | 109 | 63% helix, 0% strand | P22943 |
Compared structures
- 4AXP · NMR structure of Hsp12, a protein induced by and required for dietary restriction-induced… · the same entry in another collection · chain A against A, TM-score 1.00
- P22943 · AlphaFold monomer V2.0 prediction for 12 kda heat shock protein (P22943) · a predicted model of the same protein · chain A against A, TM-score 0.32
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 P22943
- Elsewhere: RCSB PDB 4AXP · PDBe 4AXP · UniProt P22943
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