5wy5

X-ray diffraction
2.92Å resolution

Crystal structure of MAGEG1 and NSE1 complex

Released:
Source organism: Homo sapiens
Primary publication:
MAGE-RING protein complexes comprise a family of E3 ubiquitin ligases.
Mol Cell 39 963-74 (2010)
PMID: 20864041

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:
Cellular component:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
PDBe Complex ID:
PDB-CPX-186729 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Non-structural maintenance of chromosomes element 3 homolog Chain: B
Molecule details ›
Chain: B
Length: 217 amino acids
Theoretical weight: 25.52 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q96MG7 (Residues: 78-294; Coverage: 71%)
Gene names: HCA4, MAGEG1, NDNL2, NSMCE3
Sequence domains: MAGE homology domain
Non-structural maintenance of chromosomes element 1 homolog Chain: A
Molecule details ›
Chain: A
Length: 238 amino acids
Theoretical weight: 27.6 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q8WV22 (Residues: 9-246; Coverage: 90%)
Gene names: HSPC333, HSPC337, NSMCE1
Sequence domains:
Structure domains:

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BSRF BEAMLINE 1W2B, SPRING-8 BEAMLINE BL38B1
Spacegroup: P21212
Unit cell:
a: 83.257Å b: 154.327Å c: 53.726Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.219 0.216 0.27
Expression system: Escherichia coli BL21(DE3)