› 3ee5

X-ray diffraction
2.2Å resolution

Crystal structure of human M340H-Beta1,4-Galactosyltransferase-I (M340H-B4GAL-T1) in complex with GLCNAC-Beta1,3-Gal-Beta-Naphthalenemethanol

Released:
DOI: 10.2210/pdb3ee5/pdb
Model geometry
Fit model/data
PDB entry 3ee5 coloured by chain, front view.
PDB entry 3ee5 coloured by chain, side view.
PDB entry 3ee5 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Deoxygenated disaccharide analogs as specific inhibitors of beta1-4-galactosyltransferase 1 and selectin-mediated tumor metastasis.
Brown JR, Yang F, Sinha A, Ramakrishnan B, Tor Y, Qasba PK, Esko JD
J Biol Chem 284 4952-9 (2009)
PMID: 19106107

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

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-147296 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
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
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: GAL, NAG
Carbohydrate polymer
7 bound ligands:
Ligand UDH 3 x UDH
Ligand 2NA 3 x 2NA
Ligand SO4 14 x SO4
Ligand MN 3 x MN
Ligand GOL 7 x GOL
Ligand DIO 1 x DIO
Ligand MES 1 x MES
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: RIGAKU RU200
Spacegroup: C2221
Unit cell:
a: 107.127Å b: 195.742Å c: 143.801Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.206 0.206 0.24
Expression system: Escherichia coli

Quick links

Citations

8 review citations

Developing inhibitors of glycan processing enzymes as tools for enabling glycobiology.
Gloster et al. (2012)
7 more

2 mentions without citation

Structural and mechanistic basis for a new mode of glycosyltransferase inhibition.
Pesnot et al. (2010)
1 more