4zlc

X-ray diffraction
2.7Å resolution

Crystal structure of the ROQ domain of human Roquin-2

Released:
Source organism: Homo sapiens
Primary publication:
Structure of human Roquin-2 and its complex with constitutive-decay element RNA.
Acta Crystallogr F Struct Biol Commun 71 1048-54 (2015)
PMID: 26249698

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:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-190743 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Roquin-2 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 155 amino acids
Theoretical weight: 17.59 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9HBD1 (Residues: 171-325; Coverage: 13%)
Gene names: MNAB, RC3H2, RNF164
Sequence domains:
Structure domains: Four Helix Bundle (Hemerythrin (Met), subunit A)

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL41XU
Spacegroup: P212121
Unit cell:
a: 60.76Å b: 60.868Å c: 169.5Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.226 0.224 0.26
Expression system: Escherichia coli