2ZOG

Crystal structure of mouse carnosinase CN2 complexed with ZN and bestatin

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004180	molecular_function	carboxypeptidase activity
A	0005654	cellular_component	nucleoplasm
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0006508	biological_process	proteolysis
A	0008233	molecular_function	peptidase activity
A	0008237	molecular_function	metallopeptidase activity
A	0016787	molecular_function	hydrolase activity
A	0016805	molecular_function	dipeptidase activity
A	0046872	molecular_function	metal ion binding
A	0070573	molecular_function	metallodipeptidase activity
A	0103046	molecular_function	alanylglutamate dipeptidase activity
B	0004180	molecular_function	carboxypeptidase activity
B	0005654	cellular_component	nucleoplasm
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0006508	biological_process	proteolysis
B	0008233	molecular_function	peptidase activity
B	0008237	molecular_function	metallopeptidase activity
B	0016787	molecular_function	hydrolase activity
B	0016805	molecular_function	dipeptidase activity
B	0046872	molecular_function	metal ion binding
B	0070573	molecular_function	metallodipeptidase activity
B	0103046	molecular_function	alanylglutamate dipeptidase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	3
Details	BINDING SITE FOR RESIDUE ZN A 2001

Chain	Residue
A	ASP132
A	GLU167
A	HIS445

---

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN A 2002

Chain	Residue
A	HIS99
A	ASP132
A	GLU166
A	ASP195

---

site_id	AC3
Number of Residues	3
Details	BINDING SITE FOR RESIDUE ZN B 3001

Chain	Residue
B	HIS445
B	ASP132
B	GLU167

---

site_id	AC4
Number of Residues	3
Details	BINDING SITE FOR RESIDUE ZN B 3002

Chain	Residue
B	HIS99
B	ASP132
B	ASP195

---

site_id	AC5
Number of Residues	12
Details	BINDING SITE FOR RESIDUE BES A 1080

Chain	Residue
A	HIS99
A	ASP132
A	GLU166
A	GLU167
A	ASP195
A	TYR197
A	ARG343
A	GLU414
A	SER417
A	HIS445
B	HIS228
B	THR330

---

site_id	AC6
Number of Residues	12
Details	BINDING SITE FOR RESIDUE BES B 1081

Chain	Residue
A	HIS228
A	THR330
B	HIS99
B	ASP132
B	GLU166
B	GLU167
B	ASP195
B	TYR197
B	ARG343
B	GLU414
B	SER417
B	HIS445

---

Functional Information from PROSITE/UniProt

site_id	PS00759
Number of Residues	40
Details	ARGE_DAPE_CPG2_2 ArgE / dapE / ACY1 / CPG2 / yscS family signature 2. STDdKGpvAgwMnaleayqktgqeipvn.LrFCLegMEEsG

Chain	Residue	Details
A	SER130-GLY169

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	ACT_SITE: ACT_SITE => ECO:0000250

Chain	Residue	Details
A	ASP101
B	ASP101

---

site_id	SWS_FT_FI2
Number of Residues	2
Details	ACT_SITE: Proton acceptor => ECO:0000250

Chain	Residue	Details
A	GLU166
B	GLU166

---

site_id	SWS_FT_FI3
Number of Residues	6
Details	BINDING: BINDING => ECO:0000269|PubMed:18550540

Chain	Residue	Details
A	HIS99
A	GLU167
B	HIS99
B	ASP132
B	GLU167
A	ASP132

---

site_id	SWS_FT_FI4
Number of Residues	10
Details	BINDING: in other chain

Chain	Residue	Details
A	ASP195
A	HIS445
B	GLU166
B	ASP195
B	ARG343
B	SER417
B	HIS445
A	GLU166
A	ARG343
A	SER417

---

site_id	SWS_FT_FI5
Number of Residues	4
Details	BINDING:

Chain	Residue	Details
B	HIS228
B	THR330
A	HIS228
A	THR330

---

site_id	SWS_FT_FI6
Number of Residues	2
Details	SITE: Important for catalytic activity

Chain	Residue	Details
A	HIS228
B	HIS228

---

site_id	SWS_FT_FI7
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q6Q0N1

Chain	Residue	Details
A	SER58
B	SER58

---

site_id	SWS_FT_FI8
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q96KP4

Chain	Residue	Details
A	SER299
B	SER299

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