2C6N
Structure of human somatic angiontensin-I converting enzyme N domain with lisinopril
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 |
| B | 0006508 | biological_process | proteolysis |
| B | 0008237 | molecular_function | metallopeptidase activity |
| B | 0008241 | molecular_function | peptidyl-dipeptidase activity |
| B | 0016020 | cellular_component | membrane |
Functional Information from PROSITE/UniProt
| site_id | PS00142 |
| Number of Residues | 10 |
| Details | ZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. TVHHEMGHIQ |
| Chain | Residue | Details |
| A | THR358-GLN367 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton acceptor 1 => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000269|PubMed:12540854, ECO:0000305|PubMed:16154999, ECO:0000305|PubMed:19773553 |
| Chain | Residue | Details |
| A | ASP354 | |
| B | ASP354 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton donor 1 => ECO:0000255|PROSITE-ProRule:PRU01355 |
| Chain | Residue | Details |
| A | HIS483 | |
| B | HIS483 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000269|PubMed:16476442 |
| Chain | Residue | Details |
| A | THR194 | |
| A | VAL492 | |
| B | THR194 | |
| B | VAL492 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000269|PubMed:16476442, ECO:0000269|PubMed:20826823, ECO:0000269|PubMed:26403559, ECO:0007744|PDB:2OC2, ECO:0007744|PDB:3NXQ |
| Chain | Residue | Details |
| A | MET353 | |
| A | SER357 | |
| A | ARG381 | |
| B | MET353 | |
| B | SER357 | |
| B | ARG381 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | SITE: Not glycosylated => ECO:0000269|PubMed:20826823 |
| Chain | Residue | Details |
| A | ALA486 | |
| B | ALA486 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:20826823, ECO:0000305|PubMed:9013598 |
| Chain | Residue | Details |
| A | LEU1 | |
| B | LEU1 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 4 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16476442, ECO:0000269|PubMed:20826823, ECO:0000269|PubMed:9013598 |
| Chain | Residue | Details |
| A | ALA17 | |
| A | GLN109 | |
| B | ALA17 | |
| B | GLN109 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 2 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16476442, ECO:0000269|PubMed:20826823, ECO:0000269|PubMed:26403559, ECO:0007744|PDB:3NXQ |
| Chain | Residue | Details |
| A | ALA37 | |
| B | ALA37 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 2 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:20826823, ECO:0000269|PubMed:9013598 |
| Chain | Residue | Details |
| A | GLU74 | |
| B | GLU74 |
| site_id | SWS_FT_FI10 |
| Number of Residues | 2 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:20826823 |
| Chain | Residue | Details |
| A | SER123 | |
| B | SER123 |
| site_id | SWS_FT_FI11 |
| Number of Residues | 2 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16476442 |
| Chain | Residue | Details |
| A | SER281 | |
| B | SER281 |
| site_id | SWS_FT_FI12 |
| Number of Residues | 2 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:20826823, ECO:0000269|PubMed:26403559, ECO:0007744|PDB:3NXQ |
| Chain | Residue | Details |
| A | ILE408 | |
| B | ILE408 |
| site_id | SWS_FT_FI13 |
| Number of Residues | 2 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:16476442, ECO:0000269|PubMed:20826823, ECO:0000269|PubMed:26403559, ECO:0000269|PubMed:9013598, ECO:0007744|PDB:3NXQ |
| Chain | Residue | Details |
| A | GLY472 | |
| B | GLY472 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1i1i |
| Chain | Residue | Details |
| A | GLU389 | |
| A | TYR501 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1i1i |
| Chain | Residue | Details |
| B | GLU389 | |
| B | TYR501 |
| site_id | CSA3 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 1i1i |
| Chain | Residue | Details |
| A | HIS491 | |
| A | GLU362 | |
| A | HIS331 | |
| A | ALA332 | |
| A | TYR501 |
| site_id | CSA4 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 1i1i |
| Chain | Residue | Details |
| B | HIS491 | |
| B | GLU362 | |
| B | HIS331 | |
| B | ALA332 | |
| B | TYR501 |
| site_id | MCSA1 |
| Number of Residues | |
| Details | M-CSA 170 |
| Chain | Residue | Details |
| site_id | MCSA2 |
| Number of Residues | |
| Details | M-CSA 170 |
| Chain | Residue | Details |
