7Q27
Crystal structure of Angiotensin-1 converting enzyme C-domain in complex with dual ACE/NEP inhibitor AD011
Functional Information from GO Data
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 | ACT_SITE: Proton acceptor 2 => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000269|PubMed:12540854, ECO:0000305|PubMed:16154999, ECO:0000305|PubMed:19773553 |
| Chain | Residue | Details |
| A | GLU384 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | ACT_SITE: Proton donor 2 => ECO:0000255|PROSITE-ProRule:PRU01355 |
| Chain | Residue | Details |
| A | HIS513 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000269|PubMed:12540854 |
| Chain | Residue | Details |
| A | ARG186 | |
| A | ARG489 | |
| A | TYR224 | |
| A | TRP485 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000269|PubMed:12540854, ECO:0000269|PubMed:16476442, ECO:0000269|PubMed:23056909, ECO:0007744|PDB:4APH |
| Chain | Residue | Details |
| A | HIS383 | |
| A | HIS387 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000269|PubMed:12540854, ECO:0000269|PubMed:16476442, ECO:0000269|PubMed:23056909, ECO:0000269|PubMed:7961923, ECO:0007744|PDB:4APH |
| Chain | Residue | Details |
| A | GLU411 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000269|PubMed:12540854, ECO:0000305|PubMed:11432860 |
| Chain | Residue | Details |
| A | ARG522 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| Details | SITE: Cleavage => ECO:0000269|PubMed:7499427, ECO:0000269|PubMed:8253769 |
| Chain | Residue | Details |
| A | ARG561 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 1 |
| Details | SITE: Not glycosylated => ECO:0000269|PubMed:9013598 |
| Chain | Residue | Details |
| A | ASN620 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 1 |
| Details | SITE: Cleavage => ECO:0000269|PubMed:10769174 |
| Chain | Residue | Details |
| A | ARG627 |
| site_id | SWS_FT_FI10 |
| Number of Residues | 1 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:23056909, ECO:0007744|PDB:4APH |
| Chain | Residue | Details |
| A | ASN72 |
| site_id | SWS_FT_FI11 |
| Number of Residues | 1 |
| Details | CARBOHYD: N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:9013598 |
| Chain | Residue | Details |
| A | GLN90 |
| site_id | SWS_FT_FI12 |
| Number of Residues | 1 |
| Details | CARBOHYD: N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:23056909, ECO:0000269|PubMed:9013598, ECO:0007744|PDB:4APH |
| Chain | Residue | Details |
| A | ASN109 |
| site_id | SWS_FT_FI13 |
| Number of Residues | 3 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine; partial => ECO:0000269|PubMed:9013598 |
| Chain | Residue | Details |
| A | GLN155 | |
| A | GLN337 | |
| A | GLN586 |
Catalytic Information from CSA
| 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 |
