› 2ma6

Solution NMR

Solution NMR Structure of the RING finger domain from the Kip1 ubiquitination-promoting E3 complex protein 1 (KPC1/RNF123) from Homo sapiens, Northeast Structural Genomics Consortium (NESG) Target HR8700A

Released:
DOI: 10.2210/pdb2ma6/pdb
PDB entry 2ma6 coloured by chain, ensemble of 20 models, front view.
PDB entry 2ma6 coloured by chain, ensemble of 20 models, side view.
PDB entry 2ma6 coloured by chain, ensemble of 20 models, top view.
Source organism: Homo sapiens
Entry authors: Ramelot TA, Yang Y, Janjua H, Kohan E, Wang H, Xiao R, Acton TB, Everett JK, Montelione GT, Kennedy MA, Northeast Structural Genomics Consortium (NESG)

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-178509 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
E3 ubiquitin-protein ligase RNF123 Chain: A
Molecule details ›
Chain: A
Length: 61 amino acids
Theoretical weight: 6.88 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q5XPI4 (Residues: 1247-1304; Coverage: 4%)
Gene names: FP1477, KPC1, RNF123
Sequence domains: Zinc finger, C3HC4 type (RING finger)
Structure domains: Zinc/RING finger domain, C3HC4 (zinc finger)

Ligands and Environments

1 bound ligand:
Ligand ZN 2 x ZN
No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 96%
Refinement method: simulated annealing, null
Expression system: Escherichia coli BL21(DE3)

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