1y8r

X-ray diffraction
2.75Å resolution

SUMO E1 ACTIVATING ENZYME SAE1-SAE2-SUMO1-MG-ATP COMPLEX

Released:

Function and Biology Details

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
PDBe Complex ID:
PDB-CPX-159021 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
SUMO-activating enzyme subunit 1 Chains: A, D
Molecule details ›
Chains: A, D
Length: 346 amino acids
Theoretical weight: 38.5 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9UBE0 (Residues: 1-346; Coverage: 100%)
Gene names: AOS1, SAE1, SUA1, UBLE1A
Sequence domains: ThiF family
Structure domains: NAD(P)-binding Rossmann-like Domain
SUMO-activating enzyme subunit 2 Chains: B, E
Molecule details ›
Chains: B, E
Length: 640 amino acids
Theoretical weight: 71.28 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9UBT2 (Residues: 1-640; Coverage: 100%)
Gene names: HRIHFB2115, SAE2, UBA2, UBLE1B
Sequence domains:
Structure domains:
Small ubiquitin-related modifier 1 Chains: C, F
Molecule details ›
Chains: C, F
Length: 97 amino acids
Theoretical weight: 11.15 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P63165 (Residues: 1-97; Coverage: 96%)
Gene names: OK/SW-cl.43, SMT3C, SMT3H3, SUMO1, UBL1
Sequence domains: Ubiquitin-2 like Rad60 SUMO-like
Structure domains: Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1

Ligands and Environments

3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 31-ID
Spacegroup: P21212
Unit cell:
a: 117.197Å b: 215.151Å c: 100.87Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.221 0.22 0.276
Expression systems:
  • Escherichia coli
  • Escherichia coli BL21(DE3)