› 2mbe

Solution NMR

Backbone 1H and 15N Chemical Shift Assignments for the first domain of FAT10

Released:
DOI: 10.2210/pdb2mbe/pdb
PDB entry 2mbe coloured by chain, ensemble of 8 models, front view.
PDB entry 2mbe coloured by chain, ensemble of 8 models, side view.
PDB entry 2mbe coloured by chain, ensemble of 8 models, top view.
Source organism: Homo sapiens
Primary publication:
Disruption of FAT10-MAD2 binding inhibits tumor progression.
Theng SS, Wang W, Mah WC, Chan C, Zhuo J, Gao Y, Qin H, Lim L, Chong SS, Song J, Lee CG
Proc Natl Acad Sci U S A 111 E5282-91 (2014)
PMID: 25422469

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-127352 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ubiquitin D Chain: A
Molecule details ›
Chain: A
Length: 75 amino acids
Theoretical weight: 8.68 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: O15205 (Residues: 8-82; Coverage: 46%)
Gene names: FAT10, UBD
Sequence domains: Ubiquitin family
Structure domains: Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 34%
Refinement method: distance geometry, torsion angle dynamics, molecular dynamics
Expression system: Escherichia coli

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Citations

9 review citations

Ubiquitin-like Protein Conjugation: Structures, Chemistry, and Mechanism.
Cappadocia et al. (2018)
8 more

2 mentions without citation

Disruption of FAT10-MAD2 binding inhibits tumor progression.
Theng et al. (2014)
1 more