MolNFT v1 · #160719 · protein
Structural basis for client recognition and activity of HSP40 chaperones
6PSI · Chaperone protein dnaj 2: “Structural basis for client recognition and activity of HSP40 chaperones”. Solution nmr, 16 pockets (best druggability 0.84). MolNFT v1 #160719 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6PSI
- Type
- protein
- Length
- 1,031 residues
- Chains
- 3
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Chaperone protein dnaj 2; Alkaline phosphatase
- EC
- 3.1.3.1
- UniProt
- Q56237, A0A086VD57
- Pockets
- 16 · best druggability 0.84
Structure
solution nmr · 2 distinct chains · 13% helix, 11% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | Chaperone protein dnaj 2 | protein | 280 | 30% helix, 26% strand | Q56237 |
| B | Alkaline phosphatase (EC 3.1.3.1) | protein | 471 | 3% helix, 2% strand | A0A086VD57 |
Pockets
16 pockets found on a 1 Å grid, 11 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 943 | 0.84 | 0.85 | 86 | empty |
| 2 | 70 | 0.74 | 0.98 | 21 | empty |
| 3 | 392 | 0.72 | 0.83 | 49 | empty |
| 4 | 655 | 0.70 | 0.78 | 56 | empty |
| 5 | 611 | 0.64 | 0.75 | 59 | empty |
Interfaces
3 interfaces between chains.
- B–C · 5429 Ų buried · 124 hydrogen bonds · protein-protein
- A–B · 2458 Ų buried · 44 hydrogen bonds · protein-protein
- A–C · 1724 Ų buried · 20 hydrogen bonds · protein-protein
Compared structures
- 6PSI · Structural Basis for Client Recognition and Activity of Hsp40 Chaperones · the same entry in another collection · chain A against A, TM-score 1.00
- Q56237 · AlphaFold monomer V2.0 prediction for chaperone protein dnaj 2 (Q56237) · a predicted model of the same protein · chain C against A, TM-score 0.49
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 Q56237
- Every structure of UniProt A0A086VD57
- Elsewhere: RCSB PDB 6PSI · PDBe 6PSI · UniProt Q56237 · UniProt A0A086VD57
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