1QMU

Duck carboxypeptidase D domain II

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004180	molecular_function	carboxypeptidase activity
A	0004181	molecular_function	metallocarboxypeptidase activity
A	0005615	cellular_component	extracellular space
A	0006508	biological_process	proteolysis
A	0006518	biological_process	peptide metabolic process
A	0008237	molecular_function	metallopeptidase activity
A	0008270	molecular_function	zinc ion binding
A	0016020	cellular_component	membrane
A	0016485	biological_process	protein processing
A	0046872	molecular_function	metal ion binding

Functional Information from PROSITE/UniProt

site_id	PS00132
Number of Residues	23
Details	CARBOXYPEPT_ZN_1 Zinc carboxypeptidases, zinc-binding region 1 signature. PeFkYigNmHGnEvVGRelllnL

Chain	Residue	Details
A	PRO65-LEU87

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site_id	PS00133
Number of Residues	11
Details	CARBOXYPEPT_ZN_2 Zinc carboxypeptidases, zinc-binding region 2 signature. HGGSLVVnYPF

Chain	Residue	Details
A	HIS181-PHE191

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	ACT_SITE: Proton donor/acceptor => ECO:0000255|PROSITE-ProRule:PRU01379

Chain	Residue	Details
A	GLU272

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site_id	SWS_FT_FI2
Number of Residues	3
Details	BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01379, ECO:0000269|PubMed:10545093

Chain	Residue	Details
A	HIS74
A	GLU77
A	HIS181

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site_id	SWS_FT_FI3
Number of Residues	3
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:10545093

Chain	Residue	Details
A	ASN136
A	ASN321
A	ASN377

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