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	ACT_SITE: Nucleophile => ECO:0000255|PROSITE-ProRule:PRU10037, ECO:0000269|PubMed:22484238, ECO:0007744|PDB:3UUE, ECO:0007744|PDB:3UUF

Chain	Residue	Details
A	SER171

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site_id	SWS_FT_FI2
Number of Residues	2
Details	ACT_SITE: ACT_SITE => ECO:0000269|PubMed:22484238, ECO:0007744|PDB:3UUE, ECO:0007744|PDB:3UUF

Chain	Residue	Details
A	ASP228
A	HIS281

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site_id	SWS_FT_FI3
Number of Residues	1
Details	CARBOHYD: O-linked (Man...) threonine => ECO:0000269|PubMed:22484238, ECO:0007744|PDB:3UUE, ECO:0007744|PDB:3UUF

Chain	Residue	Details
A	THR32

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site_id	SWS_FT_FI4
Number of Residues	1
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255|PROSITE-ProRule:PRU00498, ECO:0000269|PubMed:22484238, ECO:0007744|PDB:3UUE, ECO:0007744|PDB:3UUF

Chain	Residue	Details
A	ASN253

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