6SAZ
Cleaved human 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 | 0004869 | molecular_function | cysteine-type endopeptidase inhibitor activity |
| B | 0005615 | cellular_component | extracellular space |
| 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 | 0004869 | molecular_function | cysteine-type endopeptidase inhibitor activity |
| D | 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. TIIHELMHAI |
| Chain | Residue | Details |
| A | THR89-ILE98 |
| site_id | PS01254 |
| Number of Residues | 119 |
| Details | FETUIN_1 Fetuin family signature 1. CNDsdvlavagfalrdinkdrkdgyvlrlnrvndaqeyrrgglgslfyltldvletdCHvlrkkawqdCgmriffesvygq..CkaifymnnpsrvlylaaynCtlrpvskkkiymtCpdC |
| Chain | Residue | Details |
| B | CYS36-CYS154 |
| site_id | PS01255 |
| Number of Residues | 10 |
| Details | FETUIN_2 Fetuin family signature 2. DvLETdCHvL |
| Chain | Residue | Details |
| B | ASP87-LEU96 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| 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_FI2 |
| 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_FI3 |
| 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_FI4 |
| Number of Residues | 113 |
| Details | Domain: {"description":"Cystatin fetuin-B-type 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00862","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| 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_FI6 |
| Number of Residues | 2 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"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 |
