Research workbench
The crystal structure of the protein complex of yeast HSP40 SIS1 and HSP70 SSA1
Analyse The crystal structure of the protein complex of yeast HSP40 SIS1 and HSP70 SSA1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2B26
- Type
- protein
- Length
- 433 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- SIS1 protein; Heat shock 70 kda protein cognate 2
- UniProt
- P25294, P11146
- Pockets
- 2 · best druggability 0.51
Structure
x-ray diffraction · 4 distinct chains · 11% helix, 39% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | SIS1 protein | protein | 157 | 10% helix, 45% strand | P25294 |
| B | SIS1 protein | protein | 147 | 13% helix, 41% strand | P25294 |
| C | SIS1 protein | protein | 122 | 11% helix, 30% strand | P25294 |
| D | Heat shock 70 kda protein cognate 2 | protein | 7 | 0% helix, 29% strand | P11146 |
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 105 | 0.51 | 0.81 | 20 | empty |
| 2 | 98 | 0.42 | 0.77 | 17 | empty |
Interfaces
2 interfaces between chains.
- A–B · 1068 Ų buried · 7 hydrogen bonds · protein-protein
- A–D · 374 Ų buried · 6 hydrogen bonds · protein-protein
Compared structures
- 2B26 · The crystal structure of the protein complex of yeast Hsp40 Sis1 and Hsp70 Ssa1 · the same entry in another collection · chain D against D, TM-score 1.00
- P25294 · AlphaFold monomer V2.0 prediction for protein SIS1 (P25294) · a predicted model of the same protein · chain B against A, TM-score 0.97
- P11146 · AlphaFold monomer V2.0 prediction for heat shock 70 kda protein cognate 2 (P11146) · a predicted model of the same protein · chain D against A, TM-score 0.70
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 P25294
- Every structure of UniProt P11146
- Elsewhere: RCSB PDB 2B26 · PDBe 2B26 · UniProt P25294 · UniProt P11146
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.