› 2lfe

Solution NMR

Solution NMR structure of N-terminal domain of human E3 ubiquitin-protein ligase HECW2, Northeast structural genomics consortium (NESG) target ht6306A

Released:
DOI: 10.2210/pdb2lfe/pdb
PDB entry 2lfe coloured by chain, ensemble of 16 models, front view.
PDB entry 2lfe coloured by chain, ensemble of 16 models, side view.
PDB entry 2lfe coloured by chain, ensemble of 16 models, top view.
Source organism: Homo sapiens
Entry authors: Lemak A, Yee A, Houliston S, Garcia M, Chitayat S, Dhe-Paganon S, Montelione GT, Arrowsmith C, Northeast Structural Genomics Consortium (NESG), 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:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-192844 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
E3 ubiquitin-protein ligase HECW2 Chain: A
Molecule details ›
Chain: A
Length: 138 amino acids
Theoretical weight: 15.95 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9P2P5 (Residues: 43-162; Coverage: 8%)
Gene names: HECW2, KIAA1301, NEDL2
Sequence domains: N-terminal domain of E3 ubiquitin-protein ligase HECW1 and 2
Structure domains: Immunoglobulin-like

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 89%
Refinement method: restrained molecular dynamics
Expression system: Escherichia coli

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