4S2R

Crystal structure of X-prolyl aminopeptidase from Caenorhabditis elegans: a cytosolic enzyme with a di-nuclear active site

Functional Information from GO Data

Chain	GOid	namespace	contents
P	0004177	molecular_function	aminopeptidase activity
P	0005737	cellular_component	cytoplasm
P	0006508	biological_process	proteolysis
P	0008270	molecular_function	zinc ion binding
P	0042803	molecular_function	protein homodimerization activity
P	0046872	molecular_function	metal ion binding
P	0051603	biological_process	proteolysis involved in protein catabolic process
P	0070006	molecular_function	metalloaminopeptidase activity
Q	0004177	molecular_function	aminopeptidase activity
Q	0005737	cellular_component	cytoplasm
Q	0006508	biological_process	proteolysis
Q	0008270	molecular_function	zinc ion binding
Q	0042803	molecular_function	protein homodimerization activity
Q	0046872	molecular_function	metal ion binding
Q	0051603	biological_process	proteolysis involved in protein catabolic process
Q	0070006	molecular_function	metalloaminopeptidase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ZN P 701

Chain	Residue
P	ASP424
P	HIS487
P	GLU522
P	GLU536
P	ZN702

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site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ZN P 702

Chain	Residue
P	ZN701
P	ASP413
P	ASP424
P	THR426
P	GLU536

---

site_id	AC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE ZN Q 701

Chain	Residue
Q	PHE378
Q	ASP413
Q	ASP424
Q	THR426
Q	GLU536
Q	ZN702

---

site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ZN Q 702

Chain	Residue
Q	ASP424
Q	HIS487
Q	GLU522
Q	GLU536
Q	ZN701

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	6
Details	BINDING: BINDING => ECO:0000305|PubMed:25905034, ECO:0007744|PDB:4S2T

Chain	Residue	Details
P	ARG78
P	HIS392
P	HIS496
Q	ARG78
Q	HIS392
Q	HIS496

---

site_id	SWS_FT_FI2
Number of Residues	10
Details	BINDING: BINDING => ECO:0000269|PubMed:25905034, ECO:0007744|PDB:4S2R, ECO:0007744|PDB:4S2T

Chain	Residue	Details
P	ASP413
Q	GLU536
P	ASP424
P	HIS487
P	GLU522
P	GLU536
Q	ASP413
Q	ASP424
Q	HIS487
Q	GLU522

---