4p22

X-ray diffraction
2.75Å resolution

Crystal Structure of N-terminal Fragments of E1

Released:
Source organism: Homo sapiens
Primary publication:
Expression, purification, and crystal structure of N-terminal domains of human ubiquitin-activating enzyme (E1).
Biosci. Biotechnol. Biochem. 78 1542-9 (2014)
PMID: 25209502

Function and Biology Details

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ubiquitin-like modifier-activating enzyme 1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 446 amino acids
Theoretical weight: 48.46 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P22314 (Residues: 1-439; Coverage: 42%)
Gene names: A1S9T, UBA1, UBE1
Sequence domains:
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRF BEAMLINE BL17U
Spacegroup: C2221
Unit cell:
a: 94.126Å b: 186.812Å c: 135.222Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.208 0.205 0.264
Expression system: Escherichia coli BL21(DE3)