2NSM

Crystal structure of the human carboxypeptidase N (Kininase I) catalytic domain

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004180	molecular_function	carboxypeptidase activity
A	0004181	molecular_function	metallocarboxypeptidase activity
A	0005515	molecular_function	protein binding
A	0005576	cellular_component	extracellular region
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	0010815	biological_process	bradykinin catabolic process
A	0016485	biological_process	protein processing
A	0030163	biological_process	protein catabolic process
A	0046872	molecular_function	metal ion binding
A	0051384	biological_process	response to glucocorticoid

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	PRO57-LEU79

---

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

Chain	Residue	Details
A	HIS196-TYR206

---

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	GLU288

---

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

Chain	Residue	Details
A	HIS66
A	GLU69
A	HIS196

---

site_id	SWS_FT_FI3
Number of Residues	3
Details	CARBOHYD: O-linked (GalNAc...) threonine => ECO:0000305|PubMed:17157876

Chain	Residue	Details
A	THR380
A	THR382
A	THR389

---