Structure of PDB 6g60 Chain D

Receptor sequence
>6g60D (length=505) Species: 266834 (Sinorhizobium meliloti 1021) [Search protein sequence]
KPNILIIMVDQLNGKLFPDGPADFLHAPNLKALAKRSARFHNNYTSSPLT
APARASFMAGQLPSRTRVYDNAAEYQSSIPTYAHHLRRAGYYTALSGKMH
LVGPDQLHGFEERLTTDIYPADFGWTPDYRKPGERIDWWYHNLGSVTGAG
VAEITNQMEYDDEVAFLANQKLYQLSRENDDESRRPWCLTVSFTHPHDPY
VARRKFWDLYEDCEHLTPEVGAIPLDEQDPHSQRIMLSCDYQNFDVTEEN
VRRSRRAYFANISYLDEKVGELIDTLTRTRMLDDTLILFCSDHGDMLGER
GLWFKMNFFEGSARVPLMIAGPGIAPGLHLTPTSNLDVTPTLADLAGISL
EEVRPWTDGVSLVPMVNGVERTEPVLMEYAAEASYAPLVAIREGKWKYVY
CALDPEQLFDLEADPLELTNLAENPRGPVDQATLTAFRDMRAAHWDMEAF
DAAVRESQARRWVVYEALRNGAYYPWDHQPLQKASERYMRNHMNLDTLEE
SKRYP
3D structure
PDB6g60 Structural insights into choline-O-sulfatase reveal the molecular determinants for ligand binding.
ChainD
Resolution1.84 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D14 Q15 T54 R58 K102 H104 T130 H201 D296 H297 K309
Catalytic site (residue number reindexed from 1) D10 Q11 T50 R54 K98 H100 T126 H197 D292 H293 K305
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 CHT D X54 W129 W143 H145 H201 K309 X50 W125 W139 H141 H197 K305
BS02 MG D D14 X54 D296 H297 D10 X50 D292 H293
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

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:6g60, PDBe:6g60, PDBj:6g60
PDBsum6g60
PubMed35503214
UniProtO69787|BETC_RHIME Choline-sulfatase (Gene Name=betC)

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