4S2T

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	0008233	molecular_function	peptidase activity
P	0008270	molecular_function	zinc ion binding
P	0016787	molecular_function	hydrolase activity
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	0008233	molecular_function	peptidase activity
Q	0008270	molecular_function	zinc ion binding
Q	0016787	molecular_function	hydrolase activity
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	6
Details	BINDING SITE FOR RESIDUE ZN P 701

Chain	Residue
A	01B1
P	ASP413
P	ASP424
P	THR426
P	GLU536
P	ZN702

---

site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE ZN P 702

Chain	Residue
P	GLU522
P	GLU536
P	ZN701
A	01B1
P	ASP424
P	HIS487

---

site_id	AC3
Number of Residues	7
Details	BINDING SITE FOR RESIDUE SO4 P 703

Chain	Residue
P	ASN186
P	LEU187
P	LYS190
P	LEU310
P	VAL311
P	ALA314
P	HOH827

---

site_id	AC4
Number of Residues	7
Details	BINDING SITE FOR RESIDUE SO4 P 704

Chain	Residue
P	LYS557
P	SER558
P	TRP581
P	ARG588
P	HOH860
P	HOH914
P	HOH925

---

site_id	AC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 P 705

Chain	Residue
P	GLN82
P	ASN85
P	GLN86
P	LEU390

---

site_id	AC6
Number of Residues	6
Details	BINDING SITE FOR RESIDUE ZN Q 701

Chain	Residue
B	01B1
Q	ASP413
Q	ASP424
Q	THR426
Q	GLU536
Q	ZN702

---

site_id	AC7
Number of Residues	6
Details	BINDING SITE FOR RESIDUE ZN Q 702

Chain	Residue
B	01B1
Q	ASP424
Q	HIS487
Q	GLU522
Q	GLU536
Q	ZN701

---

site_id	AC8
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 Q 703

Chain	Residue
P	GLU17
P	HOH902
Q	PRO123
Q	SER147
Q	TYR293

---

site_id	AC9
Number of Residues	7
Details	BINDING SITE FOR RESIDUE SO4 Q 704

Chain	Residue
Q	ASN186
Q	LEU187
Q	LYS190
Q	LEU310
Q	ALA314
Q	HOH833
Q	HOH975

---

site_id	BC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 Q 705

Chain	Residue
Q	GLN82
Q	ASN85
Q	GLN86
Q	LEU390

---

site_id	BC2
Number of Residues	8
Details	BINDING SITE FOR RESIDUE SO4 Q 706

Chain	Residue
Q	PHE556
Q	LYS557
Q	SER558
Q	TRP581
Q	TYR585
Q	ARG588
Q	HOH810
Q	HOH971

---

site_id	BC3
Number of Residues	18
Details	BINDING SITE FOR CHAIN A OF APSTATIN

Chain	Residue
A	HOH101
P	TYR43
P	ARG78
P	PHE378
P	ILE381
P	HIS392
P	LYS394
P	ASP413
P	ASP424
P	HIS483
P	GLY484
P	GLY486
P	HIS487
P	HIS496
P	GLU522
P	GLU536
P	ZN701
P	ZN702

---

site_id	BC4
Number of Residues	19
Details	BINDING SITE FOR CHAIN B OF APSTATIN

Chain	Residue
Q	GLU522
Q	GLU536
Q	ZN701
Q	ZN702
B	HOH101
Q	TYR43
Q	ASP76
Q	ARG78
Q	PHE378
Q	ILE381
Q	HIS392
Q	LYS394
Q	ASP413
Q	ASP424
Q	HIS483
Q	GLY484
Q	GLY486
Q	HIS487
Q	HIS496

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	6
Details	Binding site: {"evidences":[{"source":"PubMed","id":"25905034","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"4S2T","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	10
Details	Binding site: {"evidences":[{"source":"PubMed","id":"25905034","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4S2R","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4S2T","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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