6ILX

Crystal structure of PETase W159F mutant from Ideonella sakaiensis

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

Functional Information from PDB Data

site_id	AC1
Number of Residues	2
Details	binding site for residue CL A 301

Chain	Residue
A	SER207
A	HIS237

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site_id	AC2
Number of Residues	2
Details	binding site for residue NA A 302

Chain	Residue
A	TYR63
A	GLY64

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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":"PubMed","id":"29235460","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"29374183","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"29603535","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"29666242","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	2
Details	Active site: {"description":"Charge relay system","evidences":[{"source":"PubMed","id":"29235460","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"29374183","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"29603535","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"29666242","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI3
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PubMed","id":"29235460","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI4
Number of Residues	1
Details	Binding site: {"evidences":[{"source":"PubMed","id":"29235460","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"29666242","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

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