PDBe 2wdt

X-ray diffraction
2.3Å resolution

Crystal structure of Plasmodium falciparum UCHL3 in complex with the suicide inhibitor UbVME

Released:

Function and Biology Details

Reaction catalysed:
Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Ubiquitin carboxyl-terminal hydrolase isozyme L3 Chains: A, C
Molecule details ›
Chains: A, C
Length: 232 amino acids
Theoretical weight: 26.93 KDa
Source organism: Plasmodium falciparum
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q8IKM8 (Residues: 1-232; Coverage: 100%)
Gene name: PF3D7_1460400
Sequence domains: Ubiquitin carboxyl-terminal hydrolase, family 1
Structure domains:
Ubiquitin Chains: B, D
Molecule details ›
Chains: B, D
Length: 76 amino acids
Theoretical weight: 8.62 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P0CG48 (Residues: 609-683; Coverage: 11%)
Gene name: UBC
Sequence domains: Ubiquitin family
Structure domains: Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-C
Spacegroup: P21212
Unit cell:
a: 134.4Å b: 75.3Å c: 85.7Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.188 0.187 0.235
Expression system: Escherichia coli BL21(DE3)