Research workbench
The HSP15 protein fitted into the low resolution cryo-EM MAP of the 50S.NC-TRNA.HSP15 complex
Analyse The HSP15 protein fitted into the low resolution cryo-EM MAP of the… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3BBU
- Type
- protein
- Length
- 104 residues
- Chains
- 1
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Heat shock protein 15
- UniProt
- P0ACG8
Structure
electron microscopy · 1 distinct chain · 39% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Heat shock protein 15 | protein | 104 | 39% helix, 22% strand | P0ACG8 |
Compared structures
- 3BBU · The Hsp15 protein fitted into the low resolution Cryo-EM map of the 50S.nc-tRNA.Hsp15… · the same entry in another collection · chain A against A, TM-score 1.00
- P0ACG8 · AlphaFold monomer V2.0 prediction for heat shock protein 15 (P0ACG8) · a predicted model of the same protein · chain A against A, TM-score 0.96
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 P0ACG8
- Elsewhere: RCSB PDB 3BBU · PDBe 3BBU · UniProt P0ACG8
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