3dkm

X-ray diffraction
1.6Å resolution

Crystal structure of the HECTD1 CPH domain

Released:
Source organism: Homo sapiens
Entry authors: Walker JR, Qiu L, Li Y, Bountra C, Wolkstrom M, Arrowsmith CH, Edwards AM, Bochkarev A, Dhe-Paganon S, 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)
PDBe Complex ID:
PDB-CPX-193929 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
E3 ubiquitin-protein ligase HECTD1 Chain: A
Molecule details ›
Chain: A
Length: 89 amino acids
Theoretical weight: 10.04 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9ULT8 (Residues: 1271-1341; Coverage: 3%)
Gene names: HECTD1, KIAA1131
Sequence domains: Mib_herc2
Structure domains: SH3 Domains

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU FR-E SUPERBRIGHT
Spacegroup: P212121
Unit cell:
a: 33.71Å b: 45.564Å c: 51.101Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.157 0.156 0.178
Expression system: Escherichia coli BL21(DE3)