Research workbench
Plasmodium falciparum HSP70-X chaperone nucleotide binding domain in complex with Z1203107138
Analyse Plasmodium falciparum HSP70-X chaperone nucleotide binding domain in complex… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7NQS
- Type
- protein
- Length
- 768 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- K7NTP5
- Ligands
- AN2, JH1, PO4
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 386 | — | K7NTP5 |
| B | — | protein | 382 | — | K7NTP5 |
Ligands and binding sites
- AN2 · Amp phosphoramidate · ligand · 2 copies · chains A, B
- JH1 · 1-ethyl-N-[(4-fluorophenyl)methyl]-1H-pyrazole-4-carboxamide · ligand · chains A, B
- PO4 · Phosphate ion · ion · 2 copies · chains A, B
- GOL · Glycerol · additive · 12 copies · chains A, B
- PG4 · Tetraethylene glycol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 7NQS · Plasmodium falciparum Hsp70-x chaperone nucleotide binding domain in complex with… · 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 7NQS · PDBe 7NQS · UniProt K7NTP5
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