2kr1

Solution NMR

Solution NMR structure of zinc binding N-terminal domain of ubiquitin-protein ligase E3A from Homo Sapiens. Northeast Structural Genomics Consortium (NESG) target HR3662

Released:
Source organism: Homo sapiens

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-170126 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ubiquitin-protein ligase E3A Chain: A
Molecule details ›
Chain: A
Length: 82 amino acids
Theoretical weight: 9.41 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q05086 (Residues: 24-87; Coverage: 7%)
Gene names: E6AP, EPVE6AP, HPVE6A, UBE3A
Sequence domains: Amino-terminal Zinc-binding domain of ubiquitin ligase E3A
Structure domains: Ubiquitin-protein ligase E3A, N-terminal zinc-binding domain (AZUL)

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 88%
Refinement method: restrained molecular dynamics
Expression system: Escherichia coli