7V1N
Structure of the Clade 2 C. difficile TcdB in complex with its receptor TFPI
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005576 | cellular_component | extracellular region |
| A | 0006508 | biological_process | proteolysis |
| A | 0008233 | molecular_function | peptidase activity |
| A | 0008234 | molecular_function | cysteine-type peptidase activity |
| A | 0008289 | molecular_function | lipid binding |
| A | 0016740 | molecular_function | transferase activity |
| A | 0016757 | molecular_function | glycosyltransferase activity |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0020002 | cellular_component | host cell plasma membrane |
| A | 0035821 | biological_process | modulation of process of another organism |
| A | 0044164 | cellular_component | host cell cytosol |
| A | 0044175 | cellular_component | host cell endosome membrane |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0090729 | molecular_function | toxin activity |
| K | 0004867 | molecular_function | serine-type endopeptidase inhibitor activity |
| K | 0005576 | cellular_component | extracellular region |
| K | 0010466 | biological_process | negative regulation of peptidase activity |
| K | 0030414 | molecular_function | peptidase inhibitor activity |
Functional Information from PROSITE/UniProt
| site_id | PS00280 |
| Number of Residues | 19 |
| Details | BPTI_KUNITZ_1 Pancreatic trypsin inhibitor (Kunitz) family signature. FiyGGCegnqnrFesleeC |
| Chain | Residue | Details |
| K | PHE82-CYS100 | |
| K | PHE153-CYS171 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 373 |
| Details | Domain: {"description":"GT44","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 207 |
| Details | Domain: {"description":"Peptidase C80","evidences":[{"source":"PROSITE-ProRule","id":"PRU01107","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 19 |
| Details | Repeat: {"description":"Cell wall-binding 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00591","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 19 |
| Details | Repeat: {"description":"Cell wall-binding 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00591","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 19 |
| Details | Repeat: {"description":"Cell wall-binding 3","evidences":[{"source":"PROSITE-ProRule","id":"PRU00591","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 19 |
| Details | Repeat: {"description":"Cell wall-binding 4","evidences":[{"source":"PROSITE-ProRule","id":"PRU00591","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 19 |
| Details | Repeat: {"description":"Cell wall-binding 5","evidences":[{"source":"PROSITE-ProRule","id":"PRU00591","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 19 |
| Details | Repeat: {"description":"Cell wall-binding 6","evidences":[{"source":"PROSITE-ProRule","id":"PRU00591","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 19 |
| Details | Repeat: {"description":"Cell wall-binding 7","evidences":[{"source":"PROSITE-ProRule","id":"PRU00591","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 19 |
| Details | Repeat: {"description":"Cell wall-binding 8","evidences":[{"source":"PROSITE-ProRule","id":"PRU00591","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI11 |
| Number of Residues | 19 |
| Details | Repeat: {"description":"Cell wall-binding 9","evidences":[{"source":"PROSITE-ProRule","id":"PRU00591","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI12 |
| Number of Residues | 20 |
| Details | Repeat: {"description":"Cell wall-binding 10","evidences":[{"source":"PROSITE-ProRule","id":"PRU00591","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI13 |
| Number of Residues | 19 |
| Details | Repeat: {"description":"Cell wall-binding 11","evidences":[{"source":"PROSITE-ProRule","id":"PRU00591","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI14 |
| Number of Residues | 19 |
| Details | Repeat: {"description":"Cell wall-binding 12","evidences":[{"source":"PROSITE-ProRule","id":"PRU00591","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI15 |
| Number of Residues | 19 |
| Details | Repeat: {"description":"Cell wall-binding 13","evidences":[{"source":"PROSITE-ProRule","id":"PRU00591","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI16 |
| Number of Residues | 22 |
| Details | Repeat: {"description":"Cell wall-binding 14","evidences":[{"source":"PROSITE-ProRule","id":"PRU00591","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI17 |
| Number of Residues | 19 |
| Details | Repeat: {"description":"Cell wall-binding 15","evidences":[{"source":"PROSITE-ProRule","id":"PRU00591","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI18 |
| Number of Residues | 19 |
| Details | Repeat: {"description":"Cell wall-binding 16","evidences":[{"source":"PROSITE-ProRule","id":"PRU00591","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI19 |
| Number of Residues | 19 |
| Details | Repeat: {"description":"Cell wall-binding 17","evidences":[{"source":"PROSITE-ProRule","id":"PRU00591","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI20 |
| Number of Residues | 19 |
| Details | Repeat: {"description":"Cell wall-binding 18","evidences":[{"source":"PROSITE-ProRule","id":"PRU00591","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI21 |
| Number of Residues | 19 |
| Details | Repeat: {"description":"Cell wall-binding 19","evidences":[{"source":"PROSITE-ProRule","id":"PRU00591","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI22 |
| Number of Residues | 89 |
| Details | Region: {"description":"Four-helical bundle","evidences":[{"source":"UniProtKB","id":"Q46342","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI23 |
| Number of Residues | 373 |
| Details | Region: {"description":"Glucosyltransferase region","evidences":[{"source":"UniProtKB","id":"P18177","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI24 |
| Number of Residues | 255 |
| Details | Region: {"description":"Autoprocessing region","evidences":[{"source":"UniProtKB","id":"P18177","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI25 |
| Number of Residues | 32 |
| Details | Region: {"description":"Interaction with host frizzled receptors FZD1, FZD2 and FZD7","evidences":[{"source":"UniProtKB","id":"P18177","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI26 |
| Number of Residues | 532 |
| Details | Region: {"description":"Receptor-binding (CROPS) region","evidences":[{"source":"UniProtKB","id":"P18177","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI27 |
| Number of Residues | 1 |
| Details | Active site: {"description":"For protease activity","evidences":[{"source":"PROSITE-ProRule","id":"PRU01107","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI28 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Nucleophile; for protease activity","evidences":[{"source":"PROSITE-ProRule","id":"PRU01107","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI29 |
| Number of Residues | 18 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P18177","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI30 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P16154","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI31 |
| Number of Residues | 1 |
| Details | Site: {"description":"Cleavage; by autolysis","evidences":[{"source":"PubMed","id":"15632438","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI32 |
| Number of Residues | 50 |
| Details | Domain: {"description":"BPTI/Kunitz inhibitor 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00031","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI33 |
| Number of Residues | 1 |
| Details | Site: {"description":"Reactive bond"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI34 |
| Number of Residues | 1 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19017259","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8639592","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |






