7Y5N
Structure of 1:1 PAPP-A.ProMBP complex(half map)
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0006955 | biological_process | immune response |
| 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 | 0008237 | molecular_function | metallopeptidase activity |
| C | 0008270 | molecular_function | zinc ion binding |
| C | 0030163 | biological_process | protein catabolic process |
| C | 0032354 | biological_process | response to follicle-stimulating hormone |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0071548 | biological_process | response to dexamethasone |
| D | 0004175 | molecular_function | endopeptidase activity |
| D | 0004222 | molecular_function | metalloendopeptidase activity |
| D | 0005515 | molecular_function | protein binding |
| D | 0005576 | cellular_component | extracellular region |
| D | 0005615 | cellular_component | extracellular space |
| D | 0006508 | biological_process | proteolysis |
| D | 0007166 | biological_process | cell surface receptor signaling pathway |
| D | 0007565 | biological_process | female pregnancy |
| D | 0008237 | molecular_function | metallopeptidase activity |
| D | 0008270 | molecular_function | zinc ion binding |
| D | 0030163 | biological_process | protein catabolic process |
| D | 0032354 | biological_process | response to follicle-stimulating hormone |
| D | 0046872 | molecular_function | metal ion binding |
| D | 0071548 | biological_process | response to dexamethasone |
Functional Information from PROSITE/UniProt
| site_id | PS00142 |
| Number of Residues | 10 |
| Details | ZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. TMIHEIGHSL |
| Chain | Residue | Details |
| C | THR479-LEU488 |
| site_id | PS00615 |
| Number of Residues | 24 |
| Details | C_TYPE_LECTIN_1 C-type lectin domain signature. CValctrggh....WRRAHClrrlp.FIC |
| Chain | Residue | Details |
| A | CYS197-CYS220 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10095 |
| Chain | Residue | Details |
| C | GLU483 | |
| D | GLU483 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU10095 |
| Chain | Residue | Details |
| C | HIS482 | |
| C | HIS486 | |
| C | HIS492 | |
| D | HIS482 | |
| D | HIS486 | |
| D | HIS492 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255 |
| Chain | Residue | Details |
| C | ASN310 | |
| C | ASN745 | |
| C | ASN1142 | |
| C | ASN1385 | |
| D | ASN310 | |
| D | ASN745 | |
| D | ASN1142 | |
| D | ASN1385 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 20 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:12421832 |
| Chain | Residue | Details |
| C | ASN322 | |
| C | ASN1439 | |
| D | ASN322 | |
| D | ASN349 | |
| D | ASN400 | |
| D | ASN521 | |
| D | ASN539 | |
| D | ASN645 | |
| D | ASN946 | |
| D | ASN1146 | |
| D | ASN1243 | |
| C | ASN349 | |
| D | ASN1439 | |
| C | ASN400 | |
| C | ASN521 | |
| C | ASN539 | |
| C | ASN645 | |
| C | ASN946 | |
| C | ASN1146 | |
| C | ASN1243 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:7524900, ECO:0000269|PubMed:8507662 |
| Chain | Residue | Details |
| A | ASN86 |
