› 4puf

X-ray diffraction
3.3Å resolution

Function and Biology Details

Reaction catalysed: 
S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-112222 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
E3 ubiquitin-protein ligase SlrP Chains: A, B
Molecule details ›
Chains: A, B
Length: 637 amino acids
Theoretical weight: 72.97 KDa
Source organism: Salmonella enterica subsp. enterica serovar Typhimurium str. 14028S
Expression system: Escherichia coli
UniProt:
  • Canonical: D0ZRB2 (Residues: 141-765; Coverage: 82%)
Gene names: STM14_928, slrP
Sequence domains:
Structure domains: Ribonuclease Inhibitor
Thioredoxin Chains: C, D
Molecule details ›
Chains: C, D
Length: 117 amino acids
Theoretical weight: 13.16 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P10599 (Residues: 1-105; Coverage: 100%)
Gene names: TRDX, TRX, TRX1, TXN
Sequence domains: Thioredoxin
Structure domains: Glutaredoxin

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID29, null
Spacegroup: P212121
Unit cell:
a: 106.29Å b: 134.83Å c: 154.62Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.274 0.272 0.308
Expression system: Escherichia coli

Quick links

Citations

9 review citations

Ubiquitin Ligases: Structure, Function, and Regulation.
Zheng et al. (2017)
8 more

9 mentions without citation

The NEL Family of Bacterial E3 Ubiquitin Ligases.
Bullones-Bolaños et al. (2022)
8 more