Research workbench
Fragment-based screening of HSP70 sheds light on the functional role of ATP-binding site residues
Analyse Fragment-based screening of HSP70 sheds light on the functional role of… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5AQS
- Type
- protein
- Length
- 983 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Heat shock cognate 71 kda protein; Bag family molecular chaperone regulator 1
- EC
- 3.6.3.51
- UniProt
- P11142, Q99933
- Ligands
- 1SQ
- Pockets
- 7 · best druggability 0.72
Structure
x-ray diffraction · 4 distinct chains · 47% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Heat shock cognate 71 kda protein (EC 3.6.3.51) | protein | 382 | 37% helix, 28% strand | P11142 |
| B | Bag family molecular chaperone regulator 1 | protein | 113 | 78% helix, 0% strand | Q99933 |
| C | Heat shock cognate 71 kda protein (EC 3.6.3.51) | protein | 378 | 39% helix, 28% strand | P11142 |
| D | Bag family molecular chaperone regulator 1 | protein | 110 | 80% helix, 0% strand | Q99933 |
Ligands and binding sites
- 1SQ · Isoquinolin-1-amine · ligand · 2 copies · chains A, C
- GOL · Glycerol · additive · 8 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 823 | 0.72 | 0.77 | 77 | 1SQ |
| 2 | 656 | 0.69 | 0.77 | 69 | 1SQ |
| 3 | 301 | 0.57 | 0.77 | 33 | empty |
| 4 | 191 | 0.45 | 0.74 | 30 | empty |
| 5 | 93 | 0.36 | 0.75 | 18 | empty |
Interfaces
5 interfaces between chains.
- A–B · 1063 Ų buried · 31 hydrogen bonds · protein-protein
- C–D · 942 Ų buried · 19 hydrogen bonds · protein-protein
- A–C · 156 Ų buried · 0 hydrogen bonds · protein-protein
- B–D · 121 Ų buried · 1 hydrogen bond · protein-protein
- A–D · 71 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 5AQS · Fragment-based screening of HSP70 sheds light on the functional role of ATP-binding site… · the same entry in another collection · chain B against B, TM-score 1.00
- Q99933 · AlphaFold monomer V2.0 prediction for bag family molecular chaperone regulator 1 (Q99933) · a predicted model of the same protein · chain D against A, TM-score 0.92
- P11142 · AlphaFold monomer V2.0 prediction for heat shock cognate 71 kda protein (P11142) · a predicted model of the same protein · chain C against A, TM-score 0.83
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 P11142
- Every structure of UniProt Q99933
- Elsewhere: RCSB PDB 5AQS · PDBe 5AQS · UniProt P11142 · UniProt Q99933
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