5AMB
Crystal structure of the Angiotensin-1 converting enzyme N-domain in complex with amyloid-beta 35-42
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 | SITE: Susceptible to oxidation => ECO:0000269|PubMed:10535332 |
Chain | Residue | Details |
P | MET35 | |
Q | MET35 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | SITE: Cleavage; by gamma-secretase; site 1 => ECO:0000305|PubMed:11851430 |
Chain | Residue | Details |
P | VAL40 | |
Q | VAL40 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | SITE: Cleavage; by gamma-secretase; site 2 => ECO:0000305|PubMed:11851430 |
Chain | Residue | Details |
P | ALA42 | |
Q | ALA42 | |
B | TYR202 | |
B | ARG500 |
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 | HIS361 | |
A | HIS365 | |
A | GLU389 | |
B | HIS361 | |
B | HIS365 | |
B | GLU389 |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | SITE: Not glycosylated => ECO:0000269|PubMed:20826823 |
Chain | Residue | Details |
A | ASN494 | |
B | ASN494 |
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 | GLN9 | |
B | GLN9 |
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 | GLN25 | |
A | GLN117 | |
B | GLN25 | |
B | GLN117 |
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 | ASN45 | |
B | ASN45 |
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 | GLN82 | |
B | GLN82 |
site_id | SWS_FT_FI10 |
Number of Residues | 2 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:20826823 |
Chain | Residue | Details |
A | GLN131 | |
B | GLN131 |
site_id | SWS_FT_FI11 |
Number of Residues | 2 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16476442 |
Chain | Residue | Details |
A | GLN289 | |
B | GLN289 |
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 | ASN416 | |
B | ASN416 |
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 | ASN480 | |
B | ASN480 |