Research workbench
Stimulating state of near full-length HSP70 dnak fused with a substrate peptide
Analyse Stimulating state of near full-length HSP70 dnak fused with a substrate peptide in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7KRW
- Type
- protein
- Length
- 2,231 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Chaperone protein dnak fused with substrate peptide
- UniProt
- A0A6D2W465
- Ligands
- ATP
- Pockets
- 20 · best druggability 0.89
Structure
x-ray diffraction · 2 distinct chains · 38% helix, 30% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| C, B, D | Chaperone protein dnak fused with substrate peptide | protein | 541 | 35% helix, 31% strand | A0A6D2W465 |
| A | Chaperone protein dnak fused with substrate peptide | protein | 608 | 40% helix, 30% strand | A0A6D2W465 |
Ligands and binding sites
- ATP · Adenosine-5'-triphosphate · ligand · 4 copies · chains C, B, A, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1050 | 0.89 | 0.91 | 156 | ATP |
| 2 | 947 | 0.86 | 0.88 | 96 | ATP |
| 3 | 644 | 0.85 | 0.89 | 74 | ATP |
| 4 | 1069 | 0.80 | 0.81 | 97 | empty |
| 5 | 841 | 0.78 | 0.81 | 75 | empty |
Interfaces
5 interfaces between chains.
- B–A · 1307 Ų buried · 28 hydrogen bonds · protein-protein
- C–D · 1268 Ų buried · 18 hydrogen bonds · protein-protein
- A–D · 641 Ų buried · 8 hydrogen bonds · protein-protein
- C–B · 311 Ų buried · 5 hydrogen bonds · protein-protein
- C–A · 72 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 7KRW · Stimulating state of near full-length Hsp70 DnaK fused with a substrate peptide · the same entry in another collection · chain C against C, TM-score 1.00
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 A0A6D2W465
- Elsewhere: RCSB PDB 7KRW · PDBe 7KRW · UniProt A0A6D2W465
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