4ZRE

Crystal structure of SMG1 F278D mutant

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005576	cellular_component	extracellular region
A	0006629	biological_process	lipid metabolic process
A	0016042	biological_process	lipid catabolic process
A	0016787	molecular_function	hydrolase activity
A	0046872	molecular_function	metal ion binding

Functional Information from PROSITE/UniProt

site_id	PS00120
Number of Residues	10
Details	LIPASE_SER Lipases, serine active site. VTVIGHSLGA

Chain	Residue	Details
A	VAL165-ALA174

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	Active site: {"description":"Nucleophile","evidences":[{"source":"PROSITE-ProRule","id":"PRU10037","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"22484238","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3UUE","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3UUF","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	2
Details	Active site: {"evidences":[{"source":"PubMed","id":"22484238","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3UUE","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3UUF","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI3
Number of Residues	1
Details	Glycosylation: {"description":"O-linked (Man...) threonine","evidences":[{"source":"PubMed","id":"22484238","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3UUE","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3UUF","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI4
Number of Residues	1
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PROSITE-ProRule","id":"PRU00498","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"22484238","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3UUE","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3UUF","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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