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

---

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	78
Details	Region: {"description":"Lid covering the active site of the uncomplexed enzyme","evidences":[{"source":"UniProtKB","id":"A0A024SC78","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	2
Details	Active site: {"description":"Nucleophile","evidences":[{"source":"UniProtKB","id":"P00590","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI3
Number of Residues	2
Details	Active site: {"evidences":[{"source":"UniProtKB","id":"P00590","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI4
Number of Residues	2
Details	Active site: {"description":"Proton donor/acceptor","evidences":[{"source":"UniProtKB","id":"P00590","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	4
Details	Site: {"description":"Transition state stabilizer","evidences":[{"source":"UniProtKB","id":"A0A024SC78","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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