› 9bkr

X-ray diffraction
1.4Å resolution

Crystal structure of the Human TRIP12 WWE domain (isoform 2) in complex with ATP

Released:
DOI: 10.2210/pdb9bkr/pdb
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PDB entry 9bkr coloured by chain, front view.
PDB entry 9bkr coloured by chain, side view.
PDB entry 9bkr coloured by chain, top view.
Source organism: Homo sapiens
Entry authors: Kimani S, Dong A, Li Y, Arrowsmith CH, Edwards AM, Halabelian L, Structural Genomics Consortium (SGC)

Function and Biology Details

Reaction catalysed: 
(1a) S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [HECT-type E3 ubiquitin transferase]-L-cysteine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + S-ubiquitinyl-[HECT-type E3 ubiquitin transferase]-L-cysteine
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-274548 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
E3 ubiquitin-protein ligase TRIP12 Chain: A
Molecule details ›
Chain: A
Length: 80 amino acids
Theoretical weight: 9.09 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q14669 (Residues: 755-784, 785-806; Coverage: 3%)
  • Best match: Q14669-2 (Residues: 761-839)
Gene names: KIAA0045, TRIP12, ULF

Ligands and Environments

2 bound ligands:
Ligand ATP 1 x ATP
Ligand UNX 1 x UNX
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: APS BEAMLINE 24-ID-C
Spacegroup: P212121
Unit cell:
a: 30.351Å b: 33.492Å c: 66.081Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.164 0.162 0.208
Expression system: Escherichia coli

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