2OC2
Structure of testis ACE with RXPA380
Functional Information from GO Data
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 |