› 2zyw

X-ray diffraction
1.8Å resolution

crystal structure of mouse cytosolic sulfotransferase mSULT1D1 complex with PAP and p-nitrophenol, obtained by two-step soaking method

Released:
DOI: 10.2210/pdb2zyw/pdb
PDB entry 2zyw coloured by chain, front view.
PDB entry 2zyw coloured by chain, side view.
PDB entry 2zyw coloured by chain, top view.
Source organism: Mus musculus
Primary publication:
Snapshot of a Michaelis complex in a sulfuryl transfer reaction: Crystal structure of a mouse sulfotransferase, mSULT1D1, complexed with donor substrate and accepter substrate.
Teramoto T, Sakakibara Y, Liu MC, Suiko M, Kimura M, Kakuta Y
Biochem Biophys Res Commun 383 83-7 (2009)
PMID: 19344693

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-174865 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Sulfotransferase 1 family member D1 Chain: X
Molecule details ›
Chain: X
Length: 295 amino acids
Theoretical weight: 35.13 KDa
Source organism: Mus musculus
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q3UZZ6 (Residues: 1-295; Coverage: 100%)
Gene names: St1d1, Sult1d1
Sequence domains: Sulfotransferase domain
Structure domains: P-loop containing nucleotide triphosphate hydrolases

Ligands and Environments

3 bound ligands:
Ligand A3P 1 x A3P
Ligand NPO 2 x NPO
Ligand GOL 3 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL38B1
Spacegroup: C2
Unit cell:
a: 155.313Å b: 67.838Å c: 42.867Å
α: 90° β: 105.25° γ: 90°
R-values:
R R work R free
0.183 0.182 0.195
Expression system: Escherichia coli BL21

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Citations

1 review citation

The PAPS-independent aryl sulfotransferase and the alternative disulfide bond formation system in pathogenic bacteria.
Malojcić et al. (2010)
9 other articles

1 mention without citation

Molecular basis for the distinct functions of redox-active and FeS-transfering glutaredoxins.
Trnka et al. (2020)