› 6qhk

X-ray diffraction
1.96Å resolution

PAO-linked dimer of the catalytic domain of the human ubiquitin-conjugating enzyme UBE2S

Released:
DOI: 10.2210/pdb6qhk/pdb
PDB entry 6qhk coloured by chain, front view.
PDB entry 6qhk coloured by chain, side view.
PDB entry 6qhk coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Autoinhibition Mechanism of the Ubiquitin-Conjugating Enzyme UBE2S by Autoubiquitination.
Liess AKL, Kucerova A, Schweimer K, Yu L, Roumeliotis TI, Diebold M, Dybkov O, Sotriffer C, Urlaub H, Choudhary JS, Mansfeld J, Lorenz S
Structure 27 1195-1210.e7 (2019)
PMID: 31230944

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 analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-172569 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ubiquitin-conjugating enzyme E2 S Chains: A, B
Molecule details ›
Chains: A, B
Length: 156 amino acids
Theoretical weight: 17.39 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q16763 (Residues: 1-156; Coverage: 70%)
Gene names: E2EPF, OK/SW-cl.73, UBE2S
Sequence domains: Ubiquitin-conjugating enzyme

Ligands and Environments

3 bound ligands:
Ligand CL 1 x CL
Ligand EDO 3 x EDO
Ligand PA0 1 x PA0
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE MASSIF-3
Spacegroup: P65
Unit cell:
a: 83.15Å b: 83.15Å c: 83.125Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.191 0.189 0.223
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

3 review citations

The Role of Conformational Dynamics in the Recognition and Regulation of Ubiquitination.
Khago et al. (2020)
2 more

1 mention without citation

Widespread occurrence of covalent lysine-cysteine redox switches in proteins.
Rabe von Pappenheim et al. (2022)