› 1yf9

X-ray diffraction
2Å resolution

Structural analysis of Leishmania major ubiquitin conjugating enzyme E2

Released:
DOI: 10.2210/pdb1yf9/pdb
PDB entry 1yf9 coloured by chain, front view.
PDB entry 1yf9 coloured by chain, side view.
PDB entry 1yf9 coloured by chain, top view.
Source organism: Leishmania major
Entry author: Structural Genomics of Pathogenic Protozoa Consortium (SGPP)

Function and Biology Details

Reaction catalysed: 
S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [E2 ubiquitin-conjugating enzyme]-L-cysteine = [E1 ubiquitin-activating enzyme]-L-cysteine + S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assemblies composition:
homo trimer (preferred)
homo hexamer
Assembly name:
PDBe Complex ID:
PDB-CPX-175676 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
E2 ubiquitin-conjugating enzyme Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 171 amino acids
Theoretical weight: 19.49 KDa
Source organism: Leishmania major
Expression system: Escherichia coli
UniProt:
  • Canonical: Q4Q5L3 (Residues: 1-167; Coverage: 71%)
Gene name: LMJF_32_0700
Sequence domains: Ubiquitin-conjugating enzyme
Structure domains: Ubiquitin Conjugating Enzyme

Ligands and Environments

1 bound ligand:
Ligand CL 6 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.2.1
Spacegroup: P43212
Unit cell:
a: 114.448Å b: 114.448Å c: 139.547Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.186 0.185 0.21
Expression system: Escherichia coli

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