7QVH

The crystal structure of HotPETase, an evolved thermostable variant of IsPETase

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005576	cellular_component	extracellular region
A	0008126	molecular_function	acetylesterase activity
A	0016787	molecular_function	hydrolase activity
A	0042178	biological_process	xenobiotic catabolic process
A	0052689	molecular_function	carboxylic ester hydrolase activity
B	0005576	cellular_component	extracellular region
B	0008126	molecular_function	acetylesterase activity
B	0016787	molecular_function	hydrolase activity
B	0042178	biological_process	xenobiotic catabolic process
B	0052689	molecular_function	carboxylic ester hydrolase activity
C	0005576	cellular_component	extracellular region
C	0008126	molecular_function	acetylesterase activity
C	0016787	molecular_function	hydrolase activity
C	0042178	biological_process	xenobiotic catabolic process
C	0052689	molecular_function	carboxylic ester hydrolase activity

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	3
Details	ACT_SITE: Nucleophile => ECO:0000305|PubMed:29235460, ECO:0000305|PubMed:29374183, ECO:0000305|PubMed:29603535, ECO:0000305|PubMed:29666242

Chain	Residue	Details
A	SER160
B	SER160
C	SER160

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site_id	SWS_FT_FI2
Number of Residues	6
Details	ACT_SITE: Charge relay system => ECO:0000305|PubMed:29235460, ECO:0000305|PubMed:29374183, ECO:0000305|PubMed:29603535, ECO:0000305|PubMed:29666242

Chain	Residue	Details
A	ASP206
A	HIS237
B	ASP206
B	HIS237
C	ASP206
C	HIS237

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site_id	SWS_FT_FI3
Number of Residues	6
Details	BINDING: BINDING => ECO:0000269|PubMed:29235460

Chain	Residue	Details
A	TYR87
A	MET161
B	TYR87
B	MET161
C	TYR87
C	MET161

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site_id	SWS_FT_FI4
Number of Residues	3
Details	BINDING: BINDING => ECO:0000305|PubMed:29235460, ECO:0000305|PubMed:29666242

Chain	Residue	Details
A	TRP185
B	TRP185
C	TRP185

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