4ywq

X-ray diffraction
1.7Å resolution

Crystal structure of the ROQ domain of human Roquin-1

Released:
Source organism: Homo sapiens
Entry authors: Dong A, Zhang Q, Li Y, Tempel W, 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
Sequence domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-178324 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Roquin-1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 170 amino acids
Theoretical weight: 19.51 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q5TC82 (Residues: 159-328; Coverage: 15%)
Gene names: KIAA2025, RC3H1, RNF198
Sequence domains:
Structure domains: Four Helix Bundle (Hemerythrin (Met), subunit A)

Ligands and Environments

1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: C2
Unit cell:
a: 171.205Å b: 29.56Å c: 59.926Å
α: 90° β: 101.55° γ: 90°
R-values:
R R work R free
0.2 0.199 0.237
Expression system: Escherichia coli BL21(DE3)