2OC2

Structure of testis ACE with RXPA380

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0006508	biological_process	proteolysis
A	0008237	molecular_function	metallopeptidase activity
A	0008241	molecular_function	peptidyl-dipeptidase activity
A	0016020	cellular_component	membrane

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN A 701

Chain	Residue
A	HIS383
A	HIS387
A	GLU411
A	RX3680

---

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CL A 703

Chain	Residue
A	ARG186
A	TRP485
A	TRP486
A	ARG489

---

site_id	AC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CL A 704

Chain	Residue
A	PRO519
A	ARG522
A	HOH763
A	TYR224

---

site_id	AC4
Number of Residues	21
Details	BINDING SITE FOR RESIDUE RX3 A 680

Chain	Residue
A	GLN281
A	HIS353
A	ALA354
A	SER355
A	ALA356
A	HIS383
A	GLU384
A	HIS387
A	PHE391
A	HIS410
A	GLU411
A	ASP415
A	PHE457
A	LYS511
A	PHE512
A	HIS513
A	VAL518
A	TYR520
A	TYR523
A	ZN701
A	HOH786

---

Functional Information from PROSITE/UniProt

site_id	PS00142
Number of Residues	10
Details	ZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. VAHHEMGHIQ

Chain	Residue	Details
A	VAL380-GLN389

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	Active site: {"description":"Proton acceptor 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU01355","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"12540854","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16154999","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"19773553","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	1
Details	Active site: {"description":"Proton donor 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU01355","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU01355","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"12540854","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU01355","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"12540854","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16476442","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23056909","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4APH","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	1
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU01355","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"12540854","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16476442","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23056909","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"7961923","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4APH","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	1
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU01355","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"12540854","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11432860","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI7
Number of Residues	1
Details	Site: {"description":"Cleavage","evidences":[{"source":"PubMed","id":"7499427","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8253769","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI8
Number of Residues	1
Details	Site: {"description":"Not glycosylated","evidences":[{"source":"PubMed","id":"9013598","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI9
Number of Residues	1
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"23056909","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4APH","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI10
Number of Residues	1
Details	Glycosylation: {"description":"N-linked (GlcNAc...) (complex) asparagine","evidences":[{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9013598","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI11
Number of Residues	1
Details	Glycosylation: {"description":"N-linked (GlcNAc...) (complex) asparagine","evidences":[{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23056909","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9013598","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4APH","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI12
Number of Residues	3
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine; partial","evidences":[{"source":"PubMed","id":"9013598","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

Catalytic Information from CSA

site_id	CSA1
Number of Residues	2
Details	Annotated By Reference To The Literature 1i1i

Chain	Residue	Details
A	TYR523
A	GLU411

---

site_id	CSA2
Number of Residues	5
Details	Annotated By Reference To The Literature 1i1i

Chain	Residue	Details
A	GLU384
A	HIS353
A	HIS513
A	ALA354
A	TYR523

---

site_id	MCSA1
Number of Residues	8
Details	M-CSA 170

Chain	Residue	Details
A	HIS353	electrostatic stabiliser, hydrogen bond acceptor
A	ALA354	electrostatic stabiliser, hydrogen bond acceptor
A	HIS383	metal ligand
A	GLU384	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
A	HIS387	metal ligand
A	GLU411	metal ligand
A	HIS513	electrostatic stabiliser, hydrogen bond donor
A	TYR523	electrostatic stabiliser, hydrogen bond donor

---