› 6h3a

X-ray diffraction
5.5Å resolution

Crystal structure of the KAP1 RBCC domain in complex with the SMARCAD1 CUE1 domain.

Released:
DOI: 10.2210/pdb6h3a/pdb
PDB entry 6h3a coloured by chain, front view.
PDB entry 6h3a coloured by chain, side view.
PDB entry 6h3a coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
A Ubiquitin-Binding Domain that Binds a Structural Fold Distinct from that of Ubiquitin.
Lim M, Newman JA, Williams HL, Masino L, Aitkenhead H, Gravard AE, Gileadi O, Svejstrup JQ
Structure 27 1316-1325.e6 (2019)
PMID: 31204252

Function and Biology Details

Reactions catalysed: 
ATP + H(2)O = ADP + phosphate
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:
hetero tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-171626 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A containing DEAD/H box 1 Chains: B, D
Molecule details ›
Chains: B, D
Length: 253 amino acids
Theoretical weight: 28.8 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9H4L7 (Residues: 95-347; Coverage: 25%)
Gene names: KIAA1122, SMARCAD1
Transcription intermediary factor 1-beta Chains: A, F
Molecule details ›
Chains: A, F
Length: 382 amino acids
Theoretical weight: 42.5 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q13263 (Residues: 53-434; Coverage: 46%)
Gene names: KAP1, RNF96, TIF1B, TRIM28
Sequence domains:

Ligands and Environments

1 bound ligand:
Ligand ZN 8 x ZN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I03
Spacegroup: I23
Unit cell:
a: 299.914Å b: 299.914Å c: 299.914Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.28 0.279 0.303
Expression system: Escherichia coli

Quick links

Citations

5 review citations

Resolving the Complexity of Ubiquitin Networks.
Kliza et al. (2020)
4 more

3 mentions without citation

Does it take two to tango? RING domain self-association and activity in TRIM E3 ubiquitin ligases.
Fiorentini et al. (2020)
2 more