Research workbench
Plasmodium falciparum HSP70-X chaperone nucleotide binding domain - ADP bound state
Analyse Plasmodium falciparum HSP70-X chaperone nucleotide binding domain - ADP bound… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6S02
- Type
- protein
- Length
- 753 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Heat shock protein 70
- UniProt
- K7NTP5
- Ligands
- ADP, MG
- Pockets
- 5 · best druggability 0.79
Structure
x-ray diffraction · 2 distinct chains · 41% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Heat shock protein 70 | protein | 378 | 42% helix, 28% strand | K7NTP5 |
| B | Heat shock protein 70 | protein | 375 | 40% helix, 26% strand | K7NTP5 |
Ligands and binding sites
- ADP · Adenosine-5'-diphosphate · ligand · 2 copies · chains A, B
- MG · Magnesium ion · metal · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 598 | 0.79 | 0.85 | 71 | ADP, MG |
| 2 | 653 | 0.77 | 0.82 | 67 | ADP, MG |
| 3 | 815 | 0.66 | 0.74 | 70 | empty |
| 4 | 55 | 0.51 | 0.86 | 11 | empty |
| 5 | 188 | 0.47 | 0.76 | 23 | empty |
Interfaces
1 interface between chains.
- A–B · 390 Ų buried · 6 hydrogen bonds · protein-protein
Compared structures
- 6S02 · Plasmodium falciparum Hsp70-x chaperone nucleotide binding domain - ADP bound state · 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 K7NTP5
- Elsewhere: RCSB PDB 6S02 · PDBe 6S02 · UniProt K7NTP5
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