1zkc

X-ray diffraction
1.65Å resolution

Crystal Structure of the cyclophiln_RING domain of human peptidylprolyl isomerase (cyclophilin)-like 2 isoform b

Released:

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
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-171651 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
RING-type E3 ubiquitin-protein ligase PPIL2 Chains: A, B
Molecule details ›
Chains: A, B
Length: 197 amino acids
Theoretical weight: 22.17 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q13356 (Residues: 280-457; Coverage: 34%)
Gene name: PPIL2
Sequence domains: Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD
Structure domains:

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU FR-E
Spacegroup: P3121
Unit cell:
a: 65.028Å b: 65.028Å c: 201.79Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.158 0.156 0.194
Expression system: Escherichia coli BL21(DE3)