Structure of PDB 5fca Chain A

Receptor sequence
>5fcaA (length=426) Species: 10090 (Mus musculus) [Search protein sequence]
HKLVPLAPADRAPAVGQFWHVTDLHLDPTYHITDDRTKVCASSKGANASN
PGPFGDVLCDSPYQLILSAFDFIKNSGQEASFMIWTGDSPPHVPVPELST
GTVIKVITNMTMTVQNLFPNLQVFPALGNHDYWPQDQLPIVTSKVYSAVA
DLWKPWLGEEAISTLKKGGFYSQKVASNPGLRIISLNTNLYYGPNIMTLN
KTDPANQFEWLENTLNSSLWNKEKVYIIAHVPVGYLPYATDTPAIRQYYN
EKLLDIFRRYSSVIAGQFYGHTHRDSLMVLSDKNGNPLNSVFVAPAVTPV
KGVLQKETNNPGVRLFQYKPGDYTLLDMVQYYLNLTEANLKGESNWTLEY
VLTQAYSVADLQPKSLYALVQQFATKDSKQFLKYYHYYFVSYDSSATCDQ
HCKTLQVCAIMNLDSMSYDDCLKQHL
3D structure
PDB5fca Structural Basis for Nucleotide Hydrolysis by the Acid Sphingomyelinase-like Phosphodiesterase SMPDL3A.
ChainA
Resolution1.924 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 3.1.4.-
3.6.1.15: nucleoside-triphosphate phosphatase.
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 ZN A D42 H44 D107 H292 D23 H25 D88 H273
BS02 ZN A D107 N148 H249 H290 D88 N129 H230 H271
BS03 ZN A H111 H149 H92 H130
BS04 ZN A D260 D438 D241 D419
Gene Ontology
Molecular Function
GO:0004767 sphingomyelin phosphodiesterase activity
GO:0008081 phosphoric diester hydrolase activity
GO:0008270 zinc ion binding
GO:0016787 hydrolase activity
GO:0016887 ATP hydrolysis activity
GO:0046872 metal ion binding
Biological Process
GO:0006685 sphingomyelin catabolic process
GO:0008150 biological_process
GO:0009143 nucleoside triphosphate catabolic process
GO:0160049 negative regulation of cGAS/STING signaling pathway
Cellular Component
GO:0005576 extracellular region
GO:0005615 extracellular space

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:5fca, PDBe:5fca, PDBj:5fca
PDBsum5fca
PubMed26792860
UniProtP70158|ASM3A_MOUSE Cyclic GMP-AMP phosphodiesterase SMPDL3A (Gene Name=Smpdl3a)

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