2m85

Solution NMR

PHD Domain from Human SHPRH

Released:
Source organism: Homo sapiens
Primary publication:
PHD domain from human SHPRH.
J Biomol NMR 56 393-9 (2013)
PMID: 23907177

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:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-172139 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
E3 ubiquitin-protein ligase SHPRH Chain: A
Molecule details ›
Chain: A
Length: 73 amino acids
Theoretical weight: 8.59 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q149N8 (Residues: 652-716; Coverage: 4%)
Gene names: KIAA2023, SHPRH
Structure domains: Zinc/RING finger domain, C3HC4 (zinc finger)

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 90%
Refinement method: distance geometry
Expression system: Escherichia coli