› 4irq

X-ray diffraction
2.3Å resolution

Crystal structure of catalytic domain of human beta1,4galactosyltransferase 7 in closed conformation in complex with manganese and UDP

Released:
DOI: 10.2210/pdb4irq/pdb
PDB entry 4irq coloured by chain, front view.
PDB entry 4irq coloured by chain, side view.
PDB entry 4irq coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Crystal structures of β-1,4-galactosyltransferase 7 enzyme reveal conformational changes and substrate binding.
Tsutsui Y, Ramakrishnan B, Qasba PK
J Biol Chem 288 31963-70 (2013)
PMID: 24052259

Function and Biology Details

Reaction catalysed: 
UDP-alpha-D-galactose + O-beta-D-xylosyl-[protein] = UDP + 4-beta-D-galactosyl-O-beta-D-xylosyl-[protein]
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo dimer
Assembly name:
PDBe Complex ID:
PDB-CPX-193684 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Beta-1,4-galactosyltransferase 7 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 251 amino acids
Theoretical weight: 29.22 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9UBV7 (Residues: 81-327; Coverage: 76%)
Gene names: B4GALT7, UNQ748/PRO1478, XGALT1
Sequence domains:
Structure domains: Spore Coat Polysaccharide Biosynthesis Protein SpsA; Chain A

Ligands and Environments

3 bound ligands:
Ligand MN 4 x MN
Ligand UDP 4 x UDP
Ligand TRS 4 x TRS
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007 HF
Spacegroup: P21
Unit cell:
a: 67.122Å b: 121.532Å c: 97.137Å
α: 90° β: 95.12° γ: 90°
R-values:
R R work R free
0.187 0.185 0.237
Expression system: Escherichia coli

Quick links

Citations

10 review citations

A molecular description of cellulose biosynthesis.
McNamara et al. (2015)
9 more

5 mentions without citation

Heparan Sulfate Proteoglycans Biosynthesis and Post Synthesis Mechanisms Combine Few Enzymes and Few Core Proteins to Generate Extensive Structural and Functional Diversity.
Annaval et al. (2020)
4 more