› 1lgp

X-ray diffraction
2Å resolution

Crystal structure of the FHA domain of the Chfr mitotic checkpoint protein complexed with tungstate

Released:
DOI: 10.2210/pdb1lgp/pdb
PDB entry 1lgp coloured by chain, front view.
PDB entry 1lgp coloured by chain, side view.
PDB entry 1lgp coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Crystal structure of the FHA domain of the Chfr mitotic checkpoint protein and its complex with tungstate.
Stavridi ES, Huyen Y, Loreto IR, Scolnick DM, Halazonetis TD, Pavletich NP, Jeffrey PD
Structure 10 891-9 (2002)
PMID: 12121644

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:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-188473 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
E3 ubiquitin-protein ligase CHFR Chain: A
Molecule details ›
Chain: A
Length: 116 amino acids
Theoretical weight: 13.2 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q96EP1 (Residues: 14-128; Coverage: 17%)
Gene names: CHFR, RNF196
Sequence domains: FHA domain
Structure domains: Tumour Suppressor Smad4

Ligands and Environments

1 bound ligand:
Ligand WO4 1 x WO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: P3221
Unit cell:
a: 62.21Å b: 62.21Å c: 54.11Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.232 0.232 0.289
Expression system: Escherichia coli BL21

Quick links

Citations

6 review citations

Adenine methylation in eukaryotes: Apprehending the complex evolutionary history and functional potential of an epigenetic modification.
Iyer et al. (2016)
5 more

8 mentions without citation

Proteasomal Degradation of Zn-Dependent Hdacs: The E3-Ligases Implicated and the Designed Protacs That Enable Degradation.
Márquez-Cantudo et al. (2021)
7 more