4qn1

X-ray diffraction
2.48Å resolution

Crystal Structure of a Functionally Uncharacterized Domain of E3 Ubiquitin Ligase SHPRH

Released:
Source organism: Homo sapiens
Entry authors: Dong A, Zhang Q, Li Y, Walker JR, Guan X, Bountra C, Arrowsmith CH, Edwards AM, Tong Y, Structural Genomics Consortium (SGC)

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:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-172139 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
E3 ubiquitin-protein ligase SHPRH Chain: A
Molecule details ›
Chain: A
Length: 420 amino acids
Theoretical weight: 48.98 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q149N8 (Residues: 1000-1418; Coverage: 25%)
Gene names: KIAA2023, SHPRH
Sequence domains:

Ligands and Environments

3 bound ligands:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: P6122
Unit cell:
a: 130.624Å b: 130.624Å c: 129.571Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.227 0.226 0.257
Expression system: Escherichia coli BL21(DE3)