2fy7

X-ray diffraction
1.7Å resolution

Crystal structure of the catalytic domain of the human beta1,4-galactosyltransferase mutant M339H in apo form

Released:
Source organism: Homo sapiens

Function and Biology Details

Reactions catalysed:
UDP-alpha-D-galactose + D-glucose = UDP + lactose
UDP-alpha-D-galactose + N-acetyl-beta-D-glucosaminyl-(1->3)-beta-D-galactosyl-(1->4)-beta-D-glucosyl-(1<->1)-ceramide = UDP + beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosaminyl-(1->3)-beta-D-galactosyl-(1->4)-beta-D-glucosyl-(1<->1)-ceramide
UDP-alpha-D-galactose + N-acetyl-beta-D-glucosaminylglycopeptide = UDP + beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosaminylglycopeptide
UDP-alpha-D-galactose + N-acetyl-D-glucosamine = UDP + N-acetyllactosamine
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-147296 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Processed beta-1,4-galactosyltransferase 1 Chain: A
Molecule details ›
Chain: A
Length: 287 amino acids
Theoretical weight: 32.77 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P15291 (Residues: 126-398; Coverage: 69%)
Gene names: B4GALT1, GGTB2
Sequence domains:
Structure domains: Spore Coat Polysaccharide Biosynthesis Protein SpsA; Chain A

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: C2221
Unit cell:
a: 70.35Å b: 137.77Å c: 66.21Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.187 0.187 0.222
Expression system: Escherichia coli BL21