7UAI
Meprin alpha helix in complex with fetuin-B
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004869 | molecular_function | cysteine-type endopeptidase inhibitor activity |
A | 0005615 | cellular_component | extracellular space |
B | 0004222 | molecular_function | metalloendopeptidase activity |
B | 0006508 | biological_process | proteolysis |
B | 0008237 | molecular_function | metallopeptidase activity |
B | 0008270 | molecular_function | zinc ion binding |
B | 0016020 | cellular_component | membrane |
C | 0004222 | molecular_function | metalloendopeptidase activity |
C | 0006508 | biological_process | proteolysis |
C | 0008237 | molecular_function | metallopeptidase activity |
C | 0008270 | molecular_function | zinc ion binding |
C | 0016020 | cellular_component | membrane |
D | 0004222 | molecular_function | metalloendopeptidase activity |
D | 0006508 | biological_process | proteolysis |
D | 0008237 | molecular_function | metallopeptidase activity |
D | 0008270 | molecular_function | zinc ion binding |
D | 0016020 | cellular_component | membrane |
E | 0004222 | molecular_function | metalloendopeptidase activity |
E | 0006508 | biological_process | proteolysis |
E | 0008237 | molecular_function | metallopeptidase activity |
E | 0008270 | molecular_function | zinc ion binding |
E | 0016020 | cellular_component | membrane |
H | 0004869 | molecular_function | cysteine-type endopeptidase inhibitor activity |
H | 0005615 | cellular_component | extracellular space |
Functional Information from PROSITE/UniProt
site_id | PS00142 |
Number of Residues | 10 |
Details | ZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. IIEHEILHAL |
Chain | Residue | Details |
E | ILE152-LEU161 |
site_id | PS00740 |
Number of Residues | 41 |
Details | MAM_1 MAM domain signature. GyFMqfsTssgsaeeaal.LesriLypkrkqqCLqFfYkmtG |
Chain | Residue | Details |
E | GLY312-GLY352 |
site_id | PS01254 |
Number of Residues | 119 |
Details | FETUIN_1 Fetuin family signature 1. CNDsdvlavagfalrdinkdrkdgyvlrlnrvndaqeyrrgglgslfyltldvletdCHvlrkkawqdCgmriffesvygq..CkaifymnnpsrvlylaaynCtlrpvskkkiymtCpdC |
Chain | Residue | Details |
A | CYS36-CYS154 |
site_id | PS01255 |
Number of Residues | 10 |
Details | FETUIN_2 Fetuin family signature 2. DvLETdCHvL |
Chain | Residue | Details |
A | ASP87-LEU96 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 776 |
Details | Domain: {"description":"Peptidase M12A","evidences":[{"source":"PROSITE-ProRule","id":"PRU01211","evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 507 |
Details | Domain: {"description":"MAM","evidences":[{"source":"PROSITE-ProRule","id":"PRU00128","evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 477 |
Details | Domain: {"description":"MATH","evidences":[{"source":"PROSITE-ProRule","id":"PRU00129","evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI4 |
Number of Residues | 4 |
Details | Active site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU01211","evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI5 |
Number of Residues | 12 |
Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU01211","evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI6 |
Number of Residues | 29 |
Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI7 |
Number of Residues | 4 |
Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI8 |
Number of Residues | 19 |
Details | Region: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]} |
Chain | Residue | Details |