2CUT

CUTINASE, A LIPOLYTIC ENZYME WITH A PREFORMED OXYANION HOLE

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005576	cellular_component	extracellular region
A	0016052	biological_process	carbohydrate catabolic process
A	0016787	molecular_function	hydrolase activity
A	0050525	molecular_function	cutinase activity
A	0052689	molecular_function	carboxylic ester hydrolase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	7
Details	BINDING SITE FOR RESIDUE DEP A 401

Chain	Residue
A	HIS188
A	SER42
A	ASN84
A	TYR119
A	SER120
A	GLN121
A	LEU182

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site_id	CAT
Number of Residues	3
Details

Chain	Residue
A	SER120
A	ASP175
A	HIS188

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Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	PRO110-GLY122

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

Chain	Residue	Details
A	CYS171-HIS188

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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":"1560844","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1AGY","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	1
Details	Active site: {"evidences":[{"source":"PubMed","id":"1560844","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1AGY","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	1
Details	Active site: {"description":"Proton donor/acceptor","evidences":[{"source":"PubMed","id":"1560844","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1AGY","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	1
Details	Site: {"description":"Transition state stabilizer","evidences":[{"source":"PubMed","id":"1560844","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8286366","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8555209","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9041628","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1AGY","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1FFE","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1OXM","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2CUT","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI5
Number of Residues	1
Details	Site: {"description":"Transition state stabilizer","evidences":[{"source":"PubMed","id":"1560844","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8286366","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9041628","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1AGY","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1OXM","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2CUT","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI6
Number of Residues	1
Details	Modified residue: {"description":"N-D-glucuronoyl glycine","evidences":[{"source":"PubMed","id":"7398618","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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Catalytic Information from CSA

site_id	CSA1
Number of Residues	5
Details	Annotated By Reference To The Literature 1agy

Chain	Residue	Details
A	ASP175
A	GLN121
A	SER42
A	SER120
A	HIS188

---

site_id	MCSA1
Number of Residues	5
Details	M-CSA 631

Chain	Residue	Details
A	SER42	electrostatic stabiliser
A	SER120	covalently attached, nucleofuge, nucleophile, proton acceptor, proton donor
A	GLN121	electrostatic stabiliser
A	ASP175	electrostatic stabiliser, increase basicity
A	HIS188	proton acceptor, proton donor

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