3GBS

Crystal structure of Aspergillus oryzae cutinase

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005576	cellular_component	extracellular region
A	0016042	biological_process	lipid catabolic process
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 PROSITE/UniProt

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

Chain	Residue	Details
A	PRO116-GLY128

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

Chain	Residue	Details
A	CYS177-HIS194

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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":"19810726","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3GBS","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	1
Details	Active site: {"evidences":[{"source":"PubMed","id":"19810726","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3GBS","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI3
Number of Residues	1
Details	Active site: {"description":"Proton donor/acceptor","evidences":[{"source":"PubMed","id":"19810726","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3GBS","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI4
Number of Residues	2
Details	Site: {"description":"Transition state stabilizer","evidences":[{"source":"UniProtKB","id":"P00590","evidenceCode":"ECO:0000250"}]}

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	ASP181
A	SER48
A	SER126
A	GLN127
A	HIS194

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