MolNFT v1 · #116901 · protein
Core domain of the class II small heat-shock protein HSP 17.7 from pisum sativum
5DS1 · 17.1 kda class II heat shock protein: “Core domain of the class II small heat-shock protein HSP 17.7 from pisum sativum”. X-ray diffraction, 4 pockets (best druggability 0.78). MolNFT v1 #116901 on GenesisL1: 3D structure, binding…
- PDB
- 5DS1
- Type
- protein
- Length
- 272 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 17.1 kda class II heat shock protein
- UniProt
- P19242
- Pockets
- 4 · best druggability 0.78
Structure
x-ray diffraction · 3 distinct chains · 0% helix, 56% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 17.1 kda class II heat shock protein | protein | 92 | 0% helix, 52% strand | P19242 |
| B | 17.1 kda class II heat shock protein | protein | 90 | 0% helix, 59% strand | P19242 |
| C | 17.1 kda class II heat shock protein | protein | 90 | 0% helix, 58% strand | P19242 |
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 133 | 0.78 | 0.96 | 32 | empty |
| 2 | 116 | 0.42 | 0.77 | 21 | empty |
| 3 | 123 | 0.41 | 0.76 | 18 | empty |
| 4 | 103 | 0.35 | 0.74 | 20 | empty |
Interfaces
3 interfaces between chains.
- B–C · 1408 Ų buried · 37 hydrogen bonds · protein-protein
- A–B · 586 Ų buried · 12 hydrogen bonds · protein-protein
- A–C · 15 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 5DS1 · Core domain of the class II small heat-shock protein HSP 17.7 from Pisum sativum · the same entry in another collection · chain A against A, TM-score 1.00
- P19242 · AlphaFold monomer V2.0 prediction for 17.1 kda class II heat shock protein (P19242) · a predicted model of the same protein · chain A against A, TM-score 0.89
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 P19242
- Elsewhere: RCSB PDB 5DS1 · PDBe 5DS1 · UniProt P19242
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