› 1fp0

Solution NMR

SOLUTION STRUCTURE OF THE PHD DOMAIN FROM THE KAP-1 COREPRESSOR

Released:
DOI: 10.2210/pdb1fp0/pdb
PDB entry 1fp0 coloured by chain, front view.
PDB entry 1fp0 coloured by chain, side view.
PDB entry 1fp0 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Solution structure of the PHD domain from the KAP-1 corepressor: structural determinants for PHD, RING and LIM zinc-binding domains.
Capili AD, Schultz DC, RauscherIII FJ, Borden KL
EMBO J 20 165-77 (2001)
PMID: 11226167

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
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-171623 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Transcription intermediary factor 1-beta Chain: A
Molecule details ›
Chain: A
Length: 88 amino acids
Theoretical weight: 9.94 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q13263 (Residues: 619-679; Coverage: 7%)
Gene names: KAP1, RNF96, TIF1B, TRIM28
Sequence domains: PHD-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
Refinement method: distance geometry and simulated annealing
Expression system: Escherichia coli

Quick links

Citations

31 review citations

Ubiquitin: structures, functions, mechanisms.
Pickart et al. (2004)
30 more

7 mentions without citation

Minimal Functional Sites in Metalloproteins and Their Usage in Structural Bioinformatics.
Rosato et al. (2016)
6 more