› 2aak

X-ray diffraction
2.4Å resolution

UBIQUITIN CONJUGATING ENZYME FROM ARABIDOPSIS THALIANA

Released:
DOI: 10.2210/pdb2aak/pdb
PDB entry 2aak coloured by chain, front view.
PDB entry 2aak coloured by chain, side view.
PDB entry 2aak coloured by chain, top view.
Source organism: Arabidopsis thaliana
Primary publication:
Three-dimensional structure of a ubiquitin-conjugating enzyme (E2).
Cook WJ, Jeffrey LC, Sullivan ML, Vierstra RD
J Biol Chem 267 15116-21 (1992)
PMID: 1321826

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:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-150606 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ubiquitin-conjugating enzyme E2 1 Chain: A
Molecule details ›
Chain: A
Length: 152 amino acids
Theoretical weight: 17.3 KDa
Source organism: Arabidopsis thaliana
Expression system: Escherichia coli
UniProt:
  • Canonical: P25865 (Residues: 1-152; Coverage: 100%)
Gene names: At1g14400, F14L17.17, F14L17_35, UBC1
Sequence domains: Ubiquitin-conjugating enzyme
Structure domains: Ubiquitin Conjugating Enzyme

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: P212121
Unit cell:
a: 41.8Å b: 44.9Å c: 83.2Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.221 0.221 0.287
Expression system: Escherichia coli

Quick links

Citations

7 review citations

Proteolysis in plants: mechanisms and functions.
Vierstra RD. (1996)
6 more

3 mentions without citation

A Perspective on the (Rise and Fall of) Protein β-Turns.
de Brevern AG. (2022)
2 more