8A7D
Partial dimer complex of PAPP-A and its inhibitor STC2
Functional Information from GO Data
Chain | GOid | namespace | contents |
C | 0004175 | molecular_function | endopeptidase activity |
C | 0004222 | molecular_function | metalloendopeptidase activity |
C | 0005515 | molecular_function | protein binding |
C | 0005576 | cellular_component | extracellular region |
C | 0005615 | cellular_component | extracellular space |
C | 0006508 | biological_process | proteolysis |
C | 0007166 | biological_process | cell surface receptor signaling pathway |
C | 0007565 | biological_process | female pregnancy |
C | 0008233 | molecular_function | peptidase activity |
C | 0008237 | molecular_function | metallopeptidase activity |
C | 0008270 | molecular_function | zinc ion binding |
C | 0016787 | molecular_function | hydrolase activity |
C | 0046872 | molecular_function | metal ion binding |
P | 0005179 | molecular_function | hormone activity |
P | 0005576 | cellular_component | extracellular region |
Q | 0004175 | molecular_function | endopeptidase activity |
Q | 0004222 | molecular_function | metalloendopeptidase activity |
Q | 0005515 | molecular_function | protein binding |
Q | 0005576 | cellular_component | extracellular region |
Q | 0005615 | cellular_component | extracellular space |
Q | 0006508 | biological_process | proteolysis |
Q | 0007166 | biological_process | cell surface receptor signaling pathway |
Q | 0007565 | biological_process | female pregnancy |
Q | 0008233 | molecular_function | peptidase activity |
Q | 0008237 | molecular_function | metallopeptidase activity |
Q | 0008270 | molecular_function | zinc ion binding |
Q | 0016787 | molecular_function | hydrolase activity |
Q | 0046872 | molecular_function | metal ion binding |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 311 |
Details | Region: {"description":"Metalloprotease"} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 21 |
Details | Region: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 12 |
Details | Compositional bias: {"description":"Basic and acidic residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | Active site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU10095","evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI5 |
Number of Residues | 3 |
Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU10095","evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI6 |
Number of Residues | 3 |
Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI7 |
Number of Residues | 8 |
Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"12421832","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI8 |
Number of Residues | 61 |
Details | Domain: {"description":"Sushi 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00302","evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI9 |
Number of Residues | 67 |
Details | Domain: {"description":"Sushi 3","evidences":[{"source":"PROSITE-ProRule","id":"PRU00302","evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI10 |
Number of Residues | 80 |
Details | Domain: {"description":"Sushi 5","evidences":[{"source":"PROSITE-ProRule","id":"PRU00302","evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |