5AM8
Crystal structure of the Angiotensin-1 converting enzyme N-domain in complex with amyloid-beta 4-10
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 |
| C | 0006508 | biological_process | proteolysis |
| C | 0008237 | molecular_function | metallopeptidase activity |
| C | 0008241 | molecular_function | peptidyl-dipeptidase activity |
| C | 0016020 | cellular_component | membrane |
| D | 0006508 | biological_process | proteolysis |
| D | 0008237 | molecular_function | metallopeptidase activity |
| D | 0008241 | molecular_function | peptidyl-dipeptidase activity |
| D | 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 | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:11274207, ECO:0000269|PubMed:26898943 |
| Chain | Residue | Details |
| P | HIS6 | |
| Q | HIS6 | |
| R | HIS6 | |
| S | HIS6 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000305|PubMed:10413512, ECO:0000305|PubMed:11274207 |
| Chain | Residue | Details |
| P | TYR10 | |
| Q | TYR10 | |
| R | TYR10 | |
| S | TYR10 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | SITE: Cleavage; by ACE => ECO:0000269|PubMed:11604391, ECO:0000269|PubMed:16154999 |
| Chain | Residue | Details |
| P | ASP7 | |
| Q | ASP7 | |
| R | ASP7 | |
| S | ASP7 | |
| C | TYR202 | |
| C | ARG500 | |
| D | TYR202 | |
| D | ARG500 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | CARBOHYD: O-linked (HexNAc...) tyrosine; partial => ECO:0000269|PubMed:22576872 |
| Chain | Residue | Details |
| P | TYR10 | |
| D | HIS361 | |
| D | HIS365 | |
| D | GLU389 | |
| Q | TYR10 | |
| R | TYR10 | |
| S | TYR10 | |
| B | HIS365 | |
| B | GLU389 | |
| C | HIS361 | |
| C | HIS365 | |
| C | GLU389 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | SITE: Not glycosylated => ECO:0000269|PubMed:20826823 |
| Chain | Residue | Details |
| A | ASN494 | |
| B | ASN494 | |
| C | ASN494 | |
| D | ASN494 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 4 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:20826823, ECO:0000305|PubMed:9013598 |
| Chain | Residue | Details |
| A | GLN9 | |
| B | GLN9 | |
| C | GLN9 | |
| D | GLN9 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 8 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16476442, ECO:0000269|PubMed:20826823, ECO:0000269|PubMed:9013598 |
| Chain | Residue | Details |
| A | GLN25 | |
| A | GLN117 | |
| B | GLN25 | |
| B | GLN117 | |
| C | GLN25 | |
| C | GLN117 | |
| D | GLN25 | |
| D | GLN117 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 4 |
| 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 | ASN45 | |
| B | ASN45 | |
| C | ASN45 | |
| D | ASN45 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 4 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:20826823, ECO:0000269|PubMed:9013598 |
| Chain | Residue | Details |
| A | GLN82 | |
| B | GLN82 | |
| C | GLN82 | |
| D | GLN82 |
| site_id | SWS_FT_FI10 |
| Number of Residues | 4 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:20826823 |
| Chain | Residue | Details |
| A | ASN131 | |
| B | ASN131 | |
| C | ASN131 | |
| D | ASN131 |
| site_id | SWS_FT_FI11 |
| Number of Residues | 4 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16476442 |
| Chain | Residue | Details |
| A | GLN289 | |
| B | GLN289 | |
| C | GLN289 | |
| D | GLN289 |
| site_id | SWS_FT_FI12 |
| Number of Residues | 4 |
| 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 | ASN416 | |
| B | ASN416 | |
| C | ASN416 | |
| D | ASN416 |
| site_id | SWS_FT_FI13 |
| Number of Residues | 4 |
| 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 | ASN480 | |
| B | ASN480 | |
| C | ASN480 | |
| D | ASN480 |
