› 2ah9

X-ray diffraction
2Å resolution

Crystal Structure of Human M340H-Beta-1,4-Galactosyltransferase-I (M340H-B4Gal-T1) in Complex with Chitotriose

Released:
DOI: 10.2210/pdb2ah9/pdb
PDB entry 2ah9 coloured by chain, front view.
PDB entry 2ah9 coloured by chain, side view.
PDB entry 2ah9 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Oligosaccharide preferences of beta1,4-galactosyltransferase-I: crystal structures of Met340His mutant of human beta1,4-galactosyltransferase-I with a pentasaccharide and trisaccharides of the N-glycan moiety.
Ramasamy V, Ramakrishnan B, Boeggeman E, Ratner DM, Seeberger PH, Qasba PK
J Mol Biol 353 53-67 (2005)
PMID: 16157350

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
Sequence domains:

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo trimer
Assembly name:
PDBe Complex ID:
PDB-CPX-147296 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Processed beta-1,4-galactosyltransferase 1 Chains: A, B, C
Molecule details ›
Chains: A, B, C
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

Carbohydrate polymer : NEW Components: NAG
Carbohydrate polymer
6 bound ligands:
Ligand UDH 3 x UDH
Ligand MN 3 x MN
Ligand GOL 7 x GOL
Ligand SO4 16 x SO4
Ligand DIO 2 x DIO
Ligand MES 1 x MES
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X9B
Spacegroup: C2221
Unit cell:
a: 107.501Å b: 195.362Å c: 144.023Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.214 0.202 0.224
Expression system: Escherichia coli BL21

Quick links

Citations

4 review citations

Glycosyltransferases: structures, functions, and mechanisms.
Lairson et al. (2008)
3 more

1 mention without citation

Functional Analogy in Human Metabolism: Enzymes with Different Biological Roles or Functional Redundancy?
Piergiorge et al. (2017)