6HT9
Mouse fetuin-B in complex with crayfish astacin
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004222 | molecular_function | metalloendopeptidase activity |
A | 0006508 | biological_process | proteolysis |
A | 0008237 | molecular_function | metallopeptidase activity |
A | 0008270 | molecular_function | zinc ion binding |
B | 0004857 | molecular_function | enzyme inhibitor activity |
B | 0004866 | molecular_function | endopeptidase inhibitor activity |
B | 0004869 | molecular_function | cysteine-type endopeptidase inhibitor activity |
B | 0005576 | cellular_component | extracellular region |
B | 0005615 | cellular_component | extracellular space |
B | 0007338 | biological_process | single fertilization |
B | 0007339 | biological_process | binding of sperm to zona pellucida |
B | 0008191 | molecular_function | metalloendopeptidase inhibitor activity |
B | 0010951 | biological_process | negative regulation of endopeptidase activity |
B | 0030414 | molecular_function | peptidase inhibitor activity |
B | 0060255 | biological_process | regulation of macromolecule metabolic process |
C | 0004222 | molecular_function | metalloendopeptidase activity |
C | 0006508 | biological_process | proteolysis |
C | 0008237 | molecular_function | metallopeptidase activity |
C | 0008270 | molecular_function | zinc ion binding |
D | 0004857 | molecular_function | enzyme inhibitor activity |
D | 0004866 | molecular_function | endopeptidase inhibitor activity |
D | 0004869 | molecular_function | cysteine-type endopeptidase inhibitor activity |
D | 0005576 | cellular_component | extracellular region |
D | 0005615 | cellular_component | extracellular space |
D | 0007338 | biological_process | single fertilization |
D | 0007339 | biological_process | binding of sperm to zona pellucida |
D | 0008191 | molecular_function | metalloendopeptidase inhibitor activity |
D | 0010951 | biological_process | negative regulation of endopeptidase activity |
D | 0030414 | molecular_function | peptidase inhibitor activity |
D | 0060255 | biological_process | regulation of macromolecule metabolic process |
Functional Information from PROSITE/UniProt
site_id | PS00142 |
Number of Residues | 10 |
Details | ZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. TIIHELMHAI |
Chain | Residue | Details |
A | THR89-ILE98 |
site_id | PS01254 |
Number of Residues | 119 |
Details | FETUIN_1 Fetuin family signature 1. CNDsevlavagfalqninrdqkdgymlslnrvhdvrehyqedmgslfyltldvletdCHvlsrkaqkdCkprmfyesvygq..CkamfhinkprrvlylpaynCtlrpvskrkthttCpdC |
Chain | Residue | Details |
B | CYS39-CYS157 |
site_id | PS01255 |
Number of Residues | 10 |
Details | FETUIN_2 Fetuin family signature 2. DvLETdCHvL |
Chain | Residue | Details |
B | ASP90-LEU99 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | Propeptide: {"featureId":"PRO_0000028874"} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 396 |
Details | Domain: {"description":"Peptidase M12A","evidences":[{"source":"PROSITE-ProRule","id":"PRU01211","evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | Active site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU01211","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"1319561","evidenceCode":"ECO:0000305"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI4 |
Number of Residues | 6 |
Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU01211","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"1319561","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8756323","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI5 |
Number of Residues | 42 |
Details | Region: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI6 |
Number of Residues | 28 |
Details | Compositional bias: {"description":"Basic and acidic residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI7 |
Number of Residues | 1 |
Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q9UGM5","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI8 |
Number of Residues | 2 |
Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI9 |
Number of Residues | 2 |
Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"17330941","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI10 |
Number of Residues | 113 |
Details | Domain: {"description":"Cystatin fetuin-B-type 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00862","evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
Catalytic Information from CSA
site_id | MCSA1 |
Number of Residues | 5 |
Details | M-CSA 403 |
Chain | Residue | Details |
A | HIS92 | metal ligand |
A | GLU93 | proton shuttle (general acid/base) |
A | HIS96 | metal ligand |
A | HIS102 | metal ligand |
A | TYR149 | transition state stabiliser |
site_id | MCSA2 |
Number of Residues | 5 |
Details | M-CSA 403 |
Chain | Residue | Details |
C | HIS92 | metal ligand |
C | GLU93 | proton shuttle (general acid/base) |
C | HIS96 | metal ligand |
C | HIS102 | metal ligand |
C | TYR149 | transition state stabiliser |