MolNFT v1 · #180445 · protein
Quasi-intermediate state (Q) of a truncated HSP70 dnak fused with a substrate peptide
7KZU · Chaperone protein dnak fused with substrate peptide…: “Quasi-intermediate state (Q) of a truncated HSP70 dnak fused with a substrate peptide”. X-ray diffraction, 3 ligands (ATP, MG, SO4), 8 pockets (best druggability 0.73). MolNFT…
- PDB
- 7KZU
- Type
- protein
- Length
- 532 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Chaperone protein dnak fused with substrate peptide, chaperone protein dnak fused with…
- UniProt
- A0A6D2W465
- Ligands
- ATP, MG, SO4
- Pockets
- 8 · best druggability 0.73
Structure
x-ray diffraction · 1 distinct chain · 34% helix, 33% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Chaperone protein dnak fused with substrate peptide, chaperone protein dnak fused with substrate peptide | protein | 532 | 34% helix, 33% strand | A0A6D2W465 |
Ligands and binding sites
- ATP · Adenosine-5'-triphosphate · ligand · chains A
- MG · Magnesium ion · metal · chains A
- SO4 · Sulfate ion · ion · chains A
- GOL · Glycerol · additive · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
8 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 364 | 0.73 | 0.85 | 54 | ATP, MG |
| 2 | 166 | 0.61 | 0.84 | 24 | GOL |
| 3 | 223 | 0.49 | 0.75 | 34 | empty |
| 4 | 101 | 0.45 | 0.79 | 19 | empty |
| 5 | 161 | 0.40 | 0.73 | 28 | empty |
Compared structures
- 7KZU · Quasi-intermediate state (Q) of a truncated Hsp70 DnaK fused with a substrate peptide · the same entry in another collection · chain A against A, 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 7KZU · PDBe 7KZU · UniProt A0A6D2W465
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