› 7oog

X-ray diffraction
2.42Å resolution

Plasmodium falciparum Hsp70-x chaperone nucleotide binding domain in complex with NCL-00023823

Released:
DOI: 10.2210/pdb7oog/pdb
PDB entry 7oog coloured by chain, front view.
PDB entry 7oog coloured by chain, side view.
PDB entry 7oog coloured by chain, top view.
Source organism: Plasmodium falciparum 3D7
Primary publication:
Structures of the Plasmodium falciparum heat-shock protein 70-x ATPase domain in complex with chemical fragments identify conserved and unique binding sites.
Mohamad N, O'Donoghue A, Kantsadi AL, Vakonakis I
Acta Crystallogr F Struct Biol Commun 77 262-268 (2021)
PMID: 34341192

Function and Biology Details

Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-125614 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Heat shock 70 kDa protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 393 amino acids
Theoretical weight: 42.83 KDa
Source organism: Plasmodium falciparum 3D7
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: K7NTP5 (Residues: 29-419; Coverage: 60%)
Gene name: PF3D7_0831700
Sequence domains: Hsp70 protein

Ligands and Environments

7 bound ligands:
Ligand GOL 13 x GOL
Ligand PG4 1 x PG4
Ligand AN2 2 x AN2
Ligand HEW 2 x HEW
Ligand PO4 2 x PO4
Ligand CL 2 x CL
Ligand MG 2 x MG
1 modified residue:
Ligand CSX 2 x CSX

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I04-1
Spacegroup: P212121
Unit cell:
a: 79.997Å b: 101.027Å c: 103.184Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.21 0.209 0.234
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

1 review citation

HSP70 and their co-chaperones in the human malaria parasite P. falciparum and their potential as drug targets.
Barth et al. (2022)
1 other article