3lrq

X-ray diffraction
2.29Å resolution

Crystal structure of the U-box domain of human ubiquitin-protein ligase (E3), NORTHEAST STRUCTURAL GENOMICS CONSORTIUM TARGET HR4604D.

Released:
Source organism: Homo sapiens
Entry authors: Kuzin A, Chen Y, Seetharaman J, Mao M, Xiao R, Ciccosanti C, Shastry R, Everett JK, Nair R, Acton TB, Rost B, Montelione GT, Tong L, Hunt JF, Northeast Structural Genomics Consortium (NESG)

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:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
PDBe Complex ID:
PDB-CPX-131805 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
E3 ubiquitin-protein ligase TRIM37 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 100 amino acids
Theoretical weight: 12.06 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: O94972 (Residues: 1-90; Coverage: 9%)
Gene names: KIAA0898, MUL, POB1, TRIM37
Structure domains: Zinc/RING finger domain, C3HC4 (zinc finger)

Ligands and Environments

1 bound ligand:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X6A
Spacegroup: P21
Unit cell:
a: 72.544Å b: 34.922Å c: 86.709Å
α: 90° β: 90.78° γ: 90°
R-values:
R R work R free
0.192 0.19 0.245
Expression system: Escherichia coli BL21(DE3)