6bsb

X-ray diffraction
1.6Å resolution

Crystal structure of the Mucin-1 SEA domain, L1105M mutant, Selenium-derivative

Released:
Source organism: Homo sapiens
Primary publication:
High-resolution structure of intramolecularly proteolyzed human mucin-1 SEA domain.
Biochim Biophys Acta Proteins Proteom 1868 140361 (2020)
PMID: 31923589

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Mucin-1 subunit alpha Chain: A
Molecule details ›
Chain: A
Length: 57 amino acids
Theoretical weight: 6.75 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P15941 (Residues: 1041-1097; Coverage: 5%)
Gene names: MUC1, PUM
Mucin-1 subunit beta Chain: B
Molecule details ›
Chain: B
Length: 55 amino acids
Theoretical weight: 6.18 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P15941 (Residues: 1098-1152; Coverage: 5%)
  • Best match: P15941-10 (Residues: 88-100)
Gene names: MUC1, PUM
Structure domains: Helix Hairpins

Ligands and Environments

No bound ligands
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X6A
Spacegroup: P3121
Unit cell:
a: 43.7Å b: 43.7Å c: 79.49Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.177 0.175 0.222
Expression system: Escherichia coli