› 2k2c

Solution NMR

Solution NMR structure of N-terminal domain of human pirh2. Northeast Structural Genomics Consortium (NESG) target HT2A

Released:
DOI: 10.2210/pdb2k2c/pdb
PDB entry 2k2c coloured by chain, ensemble of 15 models, front view.
PDB entry 2k2c coloured by chain, ensemble of 15 models, side view.
PDB entry 2k2c coloured by chain, ensemble of 15 models, top view.
Source organism: Homo sapiens
Primary publication:
Molecular basis of Pirh2-mediated p53 ubiquitylation.
Sheng Y, Laister RC, Lemak A, Wu B, Tai E, Duan S, Lukin J, Sunnerhagen M, Srisailam S, Karra M, Benchimol S, Arrowsmith CH
Nat Struct Mol Biol 15 1334-42 (2008)
PMID: 19043414

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 Chain: A
Molecule details ›
Chain: A
Length: 137 amino acids
Theoretical weight: 15.91 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q96PM5 (Residues: 1-137; Coverage: 53%)
Gene names: ARNIP, CHIMP, PIRH2, RCHY1, RNF199, ZNF363
Sequence domains: CHY zinc finger

Ligands and Environments

1 bound ligand:
Ligand ZN 6 x ZN
No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 85%
Refinement method: molecular dynamics
Expression system: Escherichia coli BL21(DE3)

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Citations

26 review citations

The tumor suppressor p53: from structures to drug discovery.
Joerger et al. (2010)
25 more

10 mentions without citation

Proteasomal Degradation of Zn-Dependent Hdacs: The E3-Ligases Implicated and the Designed Protacs That Enable Degradation.
Márquez-Cantudo et al. (2021)
9 more