Structure of PDB 6fny Chain G

Receptor sequence

>6fnyG (length=509) Species: 266834 (Sinorhizobium meliloti 1021)

GKPNILIIMVDQLNGKLFPDGPADFLHAPNLKALAKRSARFHNNYTSSPL
CAPARASFMAGQLPSRTRVYDNAAEYQSSIPTYAHHLRRAGYYTALSGKM
HFVGPDQLHGFEERLTTDIYPADFGWTPDYRKPGERIDWWYHNLGSVTGA
GVAEITNQMEYDDEVAFLANQKLYQLSRENDDESRRPWCLTVSFTHPHDP
YVARRKFWDLYEDCEHLTPEVGAIPLDEQDPHSQRIMLSCDYQNFDVTEE
NVRRSRRAYFANISYLDEKVGELIDTLTRTRMLDDTLILFCSDHGDMLGE
RGLWFKMNFFEGSARVPLMIAGPGIAPGLHLTPTSNLDVTPTLADLAGIS
LEEVRPWTDGVSLVPMVNGVERTEPVLMEYAAEASYAPLVAIREGKWKYV
YCALDPEQLFDLEADPLELTNLAENPRGPVDQATLTAFRDMRAAHWDMEA
FDAAVRESQARRWVVYEALRNGAYYPWDHQPLQKASERYMRNHMNLDTLE
ESKRYPRGE

3D structure

• PDB: 6fny Structural and Mechanistic Analysis of the Choline Sulfatase from Sinorhizobium melliloti: A Class I Sulfatase Specific for an Alkyl Sulfate Ester.
• Chain: G
• Resolution: 2.79 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): D14 Q15 C54 R58 K102 H104 T130 H201 D296 H297 K309
• Catalytic site (residue number reindexed from 1): D11 Q12 C51 R55 K99 H101 T127 H198 D293 H294 K306
• Enzyme Commision number: 3.1.6.6: choline-sulfatase.

Interaction with ligand

Site #	Ligand	Ligand chain	Binding residues on receptor (original residue number in PDB)	Binding residues on receptor (residue number reindexed from 1)	Binding affinity
BS01	CA	G	D14 C54 D296 H297	D11 C51 D293 H294

Gene Ontology

Molecular Function

• GO:0008484 sulfuric ester hydrolase activity
• GO:0016787 hydrolase activity
• GO:0046872 metal ion binding
• GO:0047753 choline-sulfatase activity

Biological Process

• GO:0042425 choline biosynthetic process

Cellular Component

• GO:0005737 cytoplasm

External links

• PDB: RCSB:6fny, PDBe:6fny, PDBj:6fny
• PDBsum: 6fny
• PubMed: 29458126
• UniProt: O69787|BETC_RHIME Choline-sulfatase (Gene Name=betC)