› 9biv

X-ray diffraction
1.68Å resolution

Crystal Structure of Ubc13 with a New Active Site Loop Conformation

Released:
DOI: 10.2210/pdb9biv/pdb
PDB entry 9biv coloured by chain, front view.
PDB entry 9biv coloured by chain, side view.
PDB entry 9biv coloured by chain, top view.
Source organism: Homo sapiens
Entry authors: Farraj RA, Edwards RA, Glover JNM

Function and Biology Details

Reaction catalysed: 
S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [E2 ubiquitin-conjugating enzyme]-L-cysteine = [E1 ubiquitin-activating enzyme]-L-cysteine + S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-158211 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Ubiquitin-conjugating enzyme E2 variant 2 Chain: A
Molecule details ›
Chain: A
Length: 145 amino acids
Theoretical weight: 16.38 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q15819 (Residues: 1-145; Coverage: 100%)
Gene names: MMS2, UBE2V2, UEV2
Sequence domains: Ubiquitin-conjugating enzyme
Ubiquitin-conjugating enzyme E2 N Chain: B
Molecule details ›
Chain: B
Length: 152 amino acids
Theoretical weight: 17.16 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P61088 (Residues: 1-152; Coverage: 100%)
Gene names: BLU, UBE2N
Sequence domains: Ubiquitin-conjugating enzyme

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007 HF
Spacegroup: C2
Unit cell:
a: 86.361Å b: 42.942Å c: 93.79Å
α: 90° β: 108.37° γ: 90°
R-values:
R R work R free
0.145 0.144 0.177
Expression system: Escherichia coli BL21(DE3)

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