PDBe 4qt6

X-ray diffraction
1.64Å resolution

Crystal structure of the SPRY domain of human HERC1

Released:
Source organism: Homo sapiens
Entry authors: Dong A, Hu J, Guan X, Wernimont A, Li Y, Bountra C, Arrowsmith CH, Edwards AM, Tong Y, 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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Probable E3 ubiquitin-protein ligase HERC1 Chain: A
Molecule details ›
Chain: A
Length: 159 amino acids
Theoretical weight: 17.99 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q15751 (Residues: 2035-2192; Coverage: 3%)
Gene name: HERC1
Sequence domains: SPRY domain
Structure domains: Jelly Rolls

Ligands and Environments

2 bound ligands:

1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU FR-E SUPERBRIGHT
Spacegroup: I23
Unit cell:
a: 99.73Å b: 99.73Å c: 99.73Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.171 0.17 0.212
Expression system: Escherichia coli BL21(DE3)