Structure of PDB 6fny Chain C

Receptor sequence
>6fnyC (length=513) Species: 266834 (Sinorhizobium meliloti 1021) [Search protein sequence]
PVTTGKPNILIIMVDQLNGKLFPDGPADFLHAPNLKALAKRSARFHNNYT
SSPLCAPARASFMAGQLPSRTRVYDNAAEYQSSIPTYAHHLRRAGYYTAL
SGKMHFVGPDQLHGFEERLTTDIYPADFGWTPDYRKPGERIDWWYHNLGS
VTGAGVAEITNQMEYDDEVAFLANQKLYQLSRENDDESRRPWCLTVSFTH
PHDPYVARRKFWDLYEDCEHLTPEVGAIPLDEQDPHSQRIMLSCDYQNFD
VTEENVRRSRRAYFANISYLDEKVGELIDTLTRTRMLDDTLILFCSDHGD
MLGERGLWFKMNFFEGSARVPLMIAGPGIAPGLHLTPTSNLDVTPTLADL
AGISLEEVRPWTDGVSLVPMVNGVERTEPVLMEYAAEASYAPLVAIREGK
WKYVYCALDPEQLFDLEADPLELTNLAENPRGPVDQATLTAFRDMRAAHW
DMEAFDAAVRESQARRWVVYEALRNGAYYPWDHQPLQKASERYMRNHMNL
DTLEESKRYPRGE
3D structure
PDB6fny Structural and Mechanistic Analysis of the Choline Sulfatase from Sinorhizobium melliloti: A Class I Sulfatase Specific for an Alkyl Sulfate Ester.
ChainC
Resolution2.79 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 C54 R58 K102 H104 T130 H201 D296 H297 K309
Catalytic site (residue number reindexed from 1) D15 Q16 C55 R59 K103 H105 T131 H202 D297 H298 K310
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 C D14 C54 D296 H297 D15 C55 D297 H298
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:6fny, PDBe:6fny, PDBj:6fny
PDBsum6fny
PubMed29458126
UniProtO69787|BETC_RHIME Choline-sulfatase (Gene Name=betC)

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