4PSE

Trichoderma reesei cutinase in complex with a C11Y4 phosphonate inhibitor

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005576	cellular_component	extracellular region
A	0016787	molecular_function	hydrolase activity
A	0050525	molecular_function	cutinase activity
B	0005576	cellular_component	extracellular region
B	0016787	molecular_function	hydrolase activity
B	0050525	molecular_function	cutinase activity

Functional Information from PROSITE/UniProt

site_id	PS00155
Number of Residues	13
Details	CUTINASE_1 Cutinase, serine active site. PnTkLVlGGYSQG

Chain	Residue	Details
A	PRO154-GLY166

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site_id	PS00931
Number of Residues	18
Details	CUTINASE_2 Cutinase, aspartate and histidine active sites. ChdgDnICqGGdiIllpH

Chain	Residue	Details
A	CYS212-HIS229

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	ACT_SITE: Nucleophile => ECO:0000250|UniProtKB:P00590

Chain	Residue	Details
A	THR208
B	THR208

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site_id	SWS_FT_FI2
Number of Residues	4
Details	SITE: Transition state stabilizer => ECO:0000250|UniProtKB:A0A024SC78

Chain	Residue	Details
A	GLY134
A	LEU209
B	GLY134
B	LEU209

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site_id	SWS_FT_FI3
Number of Residues	2
Details	ACT_SITE: Nucleophile => ECO:0000269|PubMed:25219509, ECO:0007744|PDB:4PSE

Chain	Residue	Details
A	SER164
B	SER164

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site_id	SWS_FT_FI4
Number of Residues	2
Details	ACT_SITE: ACT_SITE => ECO:0000250|UniProtKB:P00590

Chain	Residue	Details
A	ASP216
B	ASP216

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site_id	SWS_FT_FI5
Number of Residues	2
Details	ACT_SITE: Proton donor/acceptor => ECO:0000250|UniProtKB:P00590

Chain	Residue	Details
A	HIS229
B	HIS229

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site_id	SWS_FT_FI6
Number of Residues	4
Details	SITE: Transition state stabilizer => ECO:0000269|PubMed:25219509, ECO:0007744|PDB:4PSE

Chain	Residue	Details
A	THR90
A	GLN165
B	THR90
B	GLN165

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