5EBB

Structure of human sphingomyelinase phosphodiesterase like 3A (SMPDL3A) with Zn2+

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004767	molecular_function	sphingomyelin phosphodiesterase activity
A	0005515	molecular_function	protein binding
A	0005576	cellular_component	extracellular region
A	0005615	cellular_component	extracellular space
A	0006685	biological_process	sphingomyelin catabolic process
A	0008081	molecular_function	phosphoric diester hydrolase activity
A	0008270	molecular_function	zinc ion binding
A	0009143	biological_process	nucleoside triphosphate catabolic process
A	0016787	molecular_function	hydrolase activity
A	0016887	molecular_function	ATP hydrolysis activity
A	0046872	molecular_function	metal ion binding
A	0070062	cellular_component	extracellular exosome
A	0160049	biological_process	negative regulation of cGAS/STING signaling pathway
B	0004767	molecular_function	sphingomyelin phosphodiesterase activity
B	0005515	molecular_function	protein binding
B	0005576	cellular_component	extracellular region
B	0005615	cellular_component	extracellular space
B	0006685	biological_process	sphingomyelin catabolic process
B	0008081	molecular_function	phosphoric diester hydrolase activity
B	0008270	molecular_function	zinc ion binding
B	0009143	biological_process	nucleoside triphosphate catabolic process
B	0016787	molecular_function	hydrolase activity
B	0016887	molecular_function	ATP hydrolysis activity
B	0046872	molecular_function	metal ion binding
B	0070062	cellular_component	extracellular exosome
B	0160049	biological_process	negative regulation of cGAS/STING signaling pathway
C	0004767	molecular_function	sphingomyelin phosphodiesterase activity
C	0005515	molecular_function	protein binding
C	0005576	cellular_component	extracellular region
C	0005615	cellular_component	extracellular space
C	0006685	biological_process	sphingomyelin catabolic process
C	0008081	molecular_function	phosphoric diester hydrolase activity
C	0008270	molecular_function	zinc ion binding
C	0009143	biological_process	nucleoside triphosphate catabolic process
C	0016787	molecular_function	hydrolase activity
C	0016887	molecular_function	ATP hydrolysis activity
C	0046872	molecular_function	metal ion binding
C	0070062	cellular_component	extracellular exosome
C	0160049	biological_process	negative regulation of cGAS/STING signaling pathway

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	21
Details	BINDING: BINDING => ECO:0000269|PubMed:26783088

Chain	Residue	Details
A	ASP45
B	ASP110
B	ASN151
B	HIS252
B	HIS293
B	HIS295
C	ASP45
C	HIS47
C	ASP110
C	ASN151
C	HIS252
A	HIS47
C	HIS293
C	HIS295
A	ASP110
A	ASN151
A	HIS252
A	HIS293
A	HIS295
B	ASP45
B	HIS47

---

site_id	SWS_FT_FI2
Number of Residues	6
Details	BINDING: BINDING => ECO:0000305|PubMed:26783088

Chain	Residue	Details
A	HIS114
A	HIS152
B	HIS114
B	HIS152
C	HIS114
C	HIS152

---

site_id	SWS_FT_FI3
Number of Residues	3
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255, ECO:0000269|PubMed:26783088, ECO:0000269|PubMed:28104755

Chain	Residue	Details
A	ASN69
B	ASN69
C	ASN69

---

site_id	SWS_FT_FI4
Number of Residues	3
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255, ECO:0000269|PubMed:26783088

Chain	Residue	Details
A	ASN131
B	ASN131
C	ASN131

---

site_id	SWS_FT_FI5
Number of Residues	3
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:28104755

Chain	Residue	Details
A	ASN222
B	ASN222
C	ASN222

---

site_id	SWS_FT_FI6
Number of Residues	6
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255

Chain	Residue	Details
A	ASN238
A	ASN437
B	ASN238
B	ASN437
C	ASN238
C	ASN437

---

site_id	SWS_FT_FI7
Number of Residues	3
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19159218

Chain	Residue	Details
A	ASN263
B	ASN263
C	ASN263

---

site_id	SWS_FT_FI8
Number of Residues	3
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:26783088, ECO:0000269|PubMed:28104755

Chain	Residue	Details
A	ASN356
B	ASN356
C	ASN356

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