› 2ro1

Solution NMR

NMR Solution Structures of Human KAP1 PHD finger-bromodomain

Released:
DOI: 10.2210/pdb2ro1/pdb
PDB entry 2ro1 coloured by chain, ensemble of 20 models, front view.
PDB entry 2ro1 coloured by chain, ensemble of 20 models, side view.
PDB entry 2ro1 coloured by chain, ensemble of 20 models, top view.
Source organism: Homo sapiens
Primary publication:
Structural insights into human KAP1 PHD finger-bromodomain and its role in gene silencing.
Zeng L, Yap KL, Ivanov AV, Wang X, Mujtaba S, Plotnikova O, Rauscher FJ, Zhou MM
Nat Struct Mol Biol 15 626-33 (2008)
PMID: 18488044

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-171623 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Transcription intermediary factor 1-beta Chain: A
Molecule details ›
Chain: A
Length: 189 amino acids
Theoretical weight: 21.04 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q13263 (Residues: 624-812; Coverage: 23%)
Gene names: KAP1, RNF96, TIF1B, TRIM28
Sequence domains: PHD-finger

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
Refinement method: simulated annealing, torsion angle dynamics
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

39 review citations

Bromodomains as therapeutic targets.
Muller et al. (2011)
38 more

18 mentions without citation

Writers and readers of histone acetylation: structure, mechanism, and inhibition.
Marmorstein et al. (2014)
17 more