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	0016787	molecular_function	hydrolase activity
A	0030599	molecular_function	pectinesterase activity
A	0042545	biological_process	cell wall modification
A	0045490	biological_process	pectin catabolic process
A	0052689	molecular_function	carboxylic ester hydrolase activity

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

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	Active site: {"description":"Proton donor","evidences":[{"source":"UniProtKB","id":"P0C1A9","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	1
Details	Active site: {"description":"Nucleophile","evidences":[{"source":"UniProtKB","id":"P0C1A9","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	3
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"P0C1A9","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	1
Details	Site: {"description":"Transition state stabilizer","evidences":[{"source":"UniProtKB","id":"P0C1A9","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	3
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PROSITE-ProRule","id":"PRU00498","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---