PDBe 2iwg

X-ray diffraction
2.35Å resolution

COMPLEX BETWEEN THE PRYSPRY DOMAIN OF TRIM21 AND IGG FC

Released:
Source organism: Homo sapiens
Primary publication:
Structural basis for PRYSPRY-mediated tripartite motif (TRIM) protein function.
Proc. Natl. Acad. Sci. U.S.A. 104 6200-5 (2007)
PMID: 17400754

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:
hetero tetramer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
E3 ubiquitin-protein ligase TRIM21 Chains: B, E
Molecule details ›
Chains: B, E
Length: 181 amino acids
Theoretical weight: 20.6 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P19474 (Residues: 287-465; Coverage: 38%)
Gene names: RNF81, RO52, SSA1, TRIM21
Sequence domains:
Structure domains: Jelly Rolls
Immunoglobulin heavy constant gamma 1 Chains: A, D
Molecule details ›
Chains: A, D
Length: 207 amino acids
Theoretical weight: 23.55 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P01857 (Residues: 120-326; Coverage: 63%)
Gene name: IGHG1
Sequence domains: Immunoglobulin C1-set domain
Structure domains: Immunoglobulins

Ligands and Environments


No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-1
Spacegroup: P61
Unit cell:
a: 112.49Å b: 112.49Å c: 194.609Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.217 0.215 0.253
Expression system: Escherichia coli