4o2x

X-ray diffraction
2.7Å resolution

Structure of a malarial protein

Released:
Model geometry
Fit model/data

Function and Biology Details

Reaction catalysed:
Hydrolysis of proteins to small peptides in the presence of ATP and magnesium. Alpha-Casein is the usual test substrate. In the absence of ATP, only oligopeptides shorter than five residues are hydrolyzed (such as succinyl-Leu-Tyr-|-NHMec; and Leu-Tyr-Leu-|-Tyr-Trp, in which cleavage of the -Tyr-|-Leu- and -Tyr-|-Trp bonds also occurs).
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-142584 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Adaptor protein ClpS core domain-containing protein; Maltose/maltodextrin-binding periplasmic protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 507 amino acids
Theoretical weight: 56.5 KDa
Source organisms: Expression system: Escherichia coli
UniProt:
  • Canonical: P0AEX9 (Residues: 27-392; Coverage: 99%)
  • Canonical: Q8IEB2 (Residues: 71-72, 73-192; Coverage: 73%)
Gene names: JW3994, PF3D7_1320100, b4034, malE
Sequence domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: APS BEAMLINE 14-BM-C
Spacegroup: P61
Unit cell:
a: 97.85Å b: 97.85Å c: 298.24Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.189 0.185 0.239
Expression system: Escherichia coli