1XG2

Crystal structure of the complex between pectin methylesterase and its inhibitor protein

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0030599	molecular_function	pectinesterase activity
A	0042545	biological_process	cell wall modification
B	0004857	molecular_function	enzyme inhibitor activity
B	0005737	cellular_component	cytoplasm
B	0043086	biological_process	negative regulation of catalytic activity
B	0046910	molecular_function	pectinesterase inhibitor activity

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	VAL148-GLY157

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site_id	PS00800
Number of Residues	20
Details	PECTINESTERASE_1 Pectinesterase signature 1. SktryviYVKrGTYKEnveV

Chain	Residue	Details
A	SER29-VAL48

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	ACT_SITE: Proton donor => ECO:0000255|PROSITE-ProRule:PRU10040

Chain	Residue	Details
A	ASP132

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site_id	SWS_FT_FI2
Number of Residues	1
Details	ACT_SITE: Nucleophile => ECO:0000255|PROSITE-ProRule:PRU10040

Chain	Residue	Details
A	ASP153

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site_id	SWS_FT_FI3
Number of Residues	4
Details	BINDING: BINDING => ECO:0000250

Chain	Residue	Details
A	THR79
A	GLN109
A	ARG221
A	TRP223

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

Chain	Residue	Details
A	GLN131

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Catalytic Information from CSA

site_id	CSA1
Number of Residues	4
Details	Annotated By Reference To The Literature 1gq8

Chain	Residue	Details
A	GLN109
A	GLN131
A	ASP132
A	ASP153

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