2NST

Crystal structure of pectin methylesterase D178A mutant in complex with hexasaccharide II

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005576	cellular_component	extracellular region
A	0005615	cellular_component	extracellular space
A	0009279	cellular_component	cell outer membrane
A	0009405	biological_process	obsolete pathogenesis
A	0016787	molecular_function	hydrolase activity
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
A	0071555	biological_process	cell wall organization
B	0005576	cellular_component	extracellular region
B	0005615	cellular_component	extracellular space
B	0009279	cellular_component	cell outer membrane
B	0009405	biological_process	obsolete pathogenesis
B	0016787	molecular_function	hydrolase activity
B	0030599	molecular_function	pectinesterase activity
B	0042545	biological_process	cell wall modification
B	0045330	molecular_function	aspartyl esterase activity
B	0045490	biological_process	pectin catabolic process
B	0071555	biological_process	cell wall organization

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	ILE194-GLY203

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	ACT_SITE: Proton donor => ECO:0000269|PubMed:17717531

Chain	Residue	Details
A	ALA178
B	ALA178

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site_id	SWS_FT_FI2
Number of Residues	2
Details	ACT_SITE: Nucleophile => ECO:0000269|PubMed:17717531

Chain	Residue	Details
A	ASP199
B	ASP199

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site_id	SWS_FT_FI3
Number of Residues	16
Details	BINDING: BINDING => ECO:0000269|PubMed:17717531

Chain	Residue	Details
A	THR109
B	GLN153
B	ARG219
B	ASN226
B	TYR230
B	ARG267
B	TRP269
B	THR272
A	GLN153
A	ARG219
A	ASN226
A	TYR230
A	ARG267
A	TRP269
A	THR272
B	THR109

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site_id	SWS_FT_FI4
Number of Residues	2
Details	SITE: Transition state stabilizer => ECO:0000269|PubMed:17717531

Chain	Residue	Details
A	GLN177
B	GLN177

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