Solution NMR

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

Source organism: Homo sapiens

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
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)
  • 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:
No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 84%
Refinement method: molecular dynamics
Chemical shifts: BMR15700  
Expression system: Escherichia coli BL21(DE3)