4PMH

The structure of rice weevil pectin methyl esterase

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005576	cellular_component	extracellular region
A	0005615	cellular_component	extracellular space
A	0030599	molecular_function	pectinesterase activity
A	0042545	biological_process	cell wall modification
A	0045330	molecular_function	aspartyl esterase activity
A	0045490	biological_process	pectin catabolic process

Functional Information from PROSITE/UniProt

site_id	PS00503
Number of Residues	10
Details	PECTINESTERASE_2 Pectinesterase signature 2. IeGDIDFVFG

Chain	Residue	Details
A	ILE221-GLY230

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	ACT_SITE: Proton donor => ECO:0000250|UniProtKB:P0C1A9

Chain	Residue	Details
A	ASP200

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site_id	SWS_FT_FI2
Number of Residues	1
Details	ACT_SITE: Nucleophile => ECO:0000250|UniProtKB:P0C1A9

Chain	Residue	Details
A	ASP226

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site_id	SWS_FT_FI3
Number of Residues	3
Details	BINDING: BINDING => ECO:0000250|UniProtKB:P0C1A9

Chain	Residue	Details
A	GLN177
A	ARG290
A	TRP292

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site_id	SWS_FT_FI4
Number of Residues	1
Details	SITE: Transition state stabilizer => ECO:0000250|UniProtKB:P0C1A9

Chain	Residue	Details
A	GLN199

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site_id	SWS_FT_FI5
Number of Residues	3
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255|PROSITE-ProRule:PRU00498

Chain	Residue	Details
A	ASN163
A	ASN324
A	ASN360

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