5MIM
Xray structure of human furin bound with the 2,5-dideoxystreptamine derived small molecule inhibitor 1n
Functional Information from GO Data
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | binding site for residue CA A 601 |
| Chain | Residue |
| A | ASP174 |
| A | ASP179 |
| A | ASP181 |
| A | HOH736 |
| A | HOH762 |
| A | HOH1071 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | binding site for residue CA A 602 |
| Chain | Residue |
| A | ASN208 |
| A | VAL210 |
| A | GLY212 |
| A | ASP115 |
| A | ASP162 |
| A | VAL205 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | binding site for residue CA A 603 |
| Chain | Residue |
| A | ASP258 |
| A | ASP301 |
| A | GLU331 |
| A | HOH825 |
| A | HOH932 |
| A | HOH1023 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | binding site for residue NA A 604 |
| Chain | Residue |
| A | THR309 |
| A | SER311 |
| A | THR314 |
| A | SER316 |
| A | HOH867 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | binding site for residue NA A 605 |
| Chain | Residue |
| A | SER279 |
| A | GLY284 |
| A | HOH748 |
| A | HOH757 |
| A | HOH1104 |
| A | HOH1121 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | binding site for residue NA A 606 |
| Chain | Residue |
| A | SER544 |
| A | SER544 |
| A | HOH804 |
| A | HOH804 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | binding site for residue NA A 607 |
| Chain | Residue |
| A | GLU546 |
| A | GLU546 |
| A | HOH1074 |
| A | HOH1074 |
| A | HOH1089 |
| A | HOH1089 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | binding site for residue CL A 608 |
| Chain | Residue |
| A | ARG276 |
| A | TYR313 |
| A | LYS449 |
| A | TYR571 |
| site_id | AC9 |
| Number of Residues | 7 |
| Details | binding site for residue 1N A 609 |
| Chain | Residue |
| A | ARG185 |
| A | ASP191 |
| A | ASN192 |
| A | LEU227 |
| A | ASP228 |
| A | GLY229 |
| A | GLU230 |
| site_id | AD1 |
| Number of Residues | 13 |
| Details | binding site for residue 1N A 610 |
| Chain | Residue |
| A | ASP153 |
| A | HIS194 |
| A | CYS198 |
| A | LEU227 |
| A | VAL231 |
| A | GLU236 |
| A | SER253 |
| A | GLY255 |
| A | ASP264 |
| A | TYR308 |
| A | SER368 |
| A | HOH770 |
| A | HOH1025 |
Functional Information from PROSITE/UniProt
| site_id | PS00136 |
| Number of Residues | 12 |
| Details | SUBTILASE_ASP Serine proteases, subtilase family, aspartic acid active site. VSILDDGIeknH |
| Chain | Residue | Details |
| A | VAL149-HIS160 |
| site_id | PS00137 |
| Number of Residues | 11 |
| Details | SUBTILASE_HIS Serine proteases, subtilase family, histidine active site. HGTrCAGeVAA |
| Chain | Residue | Details |
| A | HIS194-ALA204 |
| site_id | PS00138 |
| Number of Residues | 11 |
| Details | SUBTILASE_SER Serine proteases, subtilase family, serine active site. GTSaSaPlAAG |
| Chain | Residue | Details |
| A | GLY366-GLY376 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 314 |
| Details | Domain: {"description":"Peptidase S8","evidences":[{"source":"PROSITE-ProRule","id":"PRU01240","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 132 |
| Details | Domain: {"description":"P/Homo B","evidences":[{"source":"PROSITE-ProRule","id":"PRU01173","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 21 |
| Details | Region: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Motif: {"description":"Cell attachment site","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 3 |
| Details | Active site: {"description":"Charge relay system","evidences":[{"source":"PROSITE-ProRule","id":"PRU01240","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 12 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"24666235","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25974265","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4OMC","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4OMD","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4RYD","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 15 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"24666235","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"25974265","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"4OMC","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4OMD","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4RYD","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 3 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |






