6qaj

X-ray diffraction
2.9Å resolution

Structure of the tripartite motif of KAP1/TRIM28

Released:

Function and Biology Details

Reactions 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
Hydrolysis of (1->4)-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in a peptidoglycan and between N-acetyl-D-glucosamine residues in chitodextrins

Structure analysis Details

Assembly composition:
homo dimer (preferred)
PDBe Complex ID:
PDB-CPX-133007 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Endolysin; Transcription intermediary factor 1-beta Chains: A, B
Molecule details ›
Chains: A, B
Length: 544 amino acids
Theoretical weight: 61.47 KDa
Source organisms: Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P00720 (Residues: 2-161; Coverage: 98%)
  • Canonical: Q13263 (Residues: 56-413; Coverage: 43%)
Gene names: E, KAP1, RNF96, TIF1B, TRIM28
Sequence domains:

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I03
Spacegroup: C2221
Unit cell:
a: 59.774Å b: 169.332Å c: 374.508Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.262 0.261 0.291
Expression system: Escherichia coli BL21(DE3)