3QPD

Structure of Aspergillus oryzae cutinase expressed in Pichia pastoris, crystallized in the presence of Paraoxon

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005576	cellular_component	extracellular region
A	0016042	biological_process	lipid 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	ACT_SITE: Nucleophile => ECO:0000269|PubMed:19810726, ECO:0007744|PDB:3GBS

Chain	Residue	Details
A	SEP126

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site_id	SWS_FT_FI2
Number of Residues	1
Details	ACT_SITE: ACT_SITE => ECO:0000269|PubMed:19810726, ECO:0007744|PDB:3GBS

Chain	Residue	Details
A	ASP181

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site_id	SWS_FT_FI3
Number of Residues	1
Details	ACT_SITE: Proton donor/acceptor => ECO:0000269|PubMed:19810726, ECO:0007744|PDB:3GBS

Chain	Residue	Details
A	HIS194

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site_id	SWS_FT_FI4
Number of Residues	2
Details	SITE: Transition state stabilizer => ECO:0000250|UniProtKB:P00590

Chain	Residue	Details
A	SER48
A	GLN127

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