› 5fq2

X-ray diffraction
2.2Å resolution

Crystal structure of human SUMO E1 UFD domain in complex with Ubc9 in a P422 space group.

Released:
DOI: 10.2210/pdb5fq2/pdb
PDB entry 5fq2 coloured by chain, front view.
PDB entry 5fq2 coloured by chain, side view.
PDB entry 5fq2 coloured by chain, top view.
Source organism: Homo sapiens
Entry authors: Liu B, Castano L, Lois M, Reverter D

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-159075 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
SUMO-conjugating enzyme UBC9 Chain: A
Molecule details ›
Chain: A
Length: 161 amino acids
Theoretical weight: 18.34 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P63279 (Residues: 1-158; Coverage: 100%)
Gene names: UBC9, UBCE9, UBE2I
Sequence domains: Ubiquitin-conjugating enzyme
Structure domains: Ubiquitin Conjugating Enzyme
SUMO-activating enzyme subunit 2 Chain: B
Molecule details ›
Chain: B
Length: 105 amino acids
Theoretical weight: 11.75 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q9UBT2 (Residues: 446-547; Coverage: 16%)
Gene names: HRIHFB2115, SAE2, UBA2, UBLE1B
Sequence domains: Ubiquitin/SUMO-activating enzyme ubiquitin-like domain
Structure domains: Ubiquitin-like 2 activating enzyme e1b. Chain: B, domain 3

Ligands and Environments

No bound ligands
2 modified residues:
Ligand LDH 1 x LDH
Ligand MLZ 1 x MLZ

Experiments and Validation Details

Entry percentile scores
X-ray source: ALBA BEAMLINE XALOC
Spacegroup: P43212
Unit cell:
a: 129.614Å b: 129.614Å c: 66.578Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.23 0.229 0.249
Expression system: Escherichia coli BL21

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