› 7ynx

X-ray diffraction
2.3Å resolution

Crystal structure of Pirh2 bound to poly-Ala peptide

Released:
DOI: 10.2210/pdb7ynx/pdb
PDB entry 7ynx coloured by chain, front view.
PDB entry 7ynx coloured by chain, side view.
PDB entry 7ynx coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Recognition of an Ala-rich C-degron by the E3 ligase Pirh2.
Wang X, Li Y, Yan X, Yang Q, Zhang B, Zhang Y, Yuan X, Jiang C, Chen D, Liu Q, Liu T, Mi W, Yu Y, Dong C
Nat Commun 14 2474 (2023)
PMID: 37120596

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
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-188669 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
RING finger and CHY zinc finger domain-containing protein 1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 203 amino acids
Theoretical weight: 22.92 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q96PM5 (Residues: 1-191; Coverage: 73%)
Gene names: ARNIP, CHIMP, PIRH2, RCHY1, RNF199, ZNF363
Sequence domains:

Ligands and Environments

3 bound ligands:
Ligand ZN 16 x ZN
Ligand SO4 5 x SO4
Ligand NA 12 x NA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRF BEAMLINE BL18U1
Spacegroup: P212121
Unit cell:
a: 69.47Å b: 80.27Å c: 84.87Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.22 0.216 0.264
Expression system: Escherichia coli

Quick links

Citations

1 citations in other articles

Molecular basis for C-degron recognition by CRL2APPBP2 ubiquitin ligase.
Zhao et al. (2023)

1 mention without citation

Recognition of an Ala-rich C-degron by the E3 ligase Pirh2.
Wang et al. (2023)