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 | 0008234 | molecular_function | cysteine-type peptidase activity |
| A | 0008289 | molecular_function | lipid binding |
| A | 0016020 | cellular_component | membrane |
| A | 0016757 | molecular_function | glycosyltransferase activity |
| A | 0020002 | cellular_component | host cell plasma membrane |
| A | 0030430 | cellular_component | host cell cytoplasm |
| A | 0035821 | biological_process | modulation of process of another organism |
| A | 0044164 | cellular_component | host cell cytosol |
| A | 0044174 | cellular_component | host cell endosome |
| 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 | 3 |
| Details | SITE: Reactive bond |
| Chain | Residue | Details |
| K | LYS64 | |
| K | ARG135 | |
| K | GLN227 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | CARBOHYD: O-linked (GalNAc...) threonine; partial => ECO:0000269|PubMed:19017259 |
| Chain | Residue | Details |
| K | THR42 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19017259, ECO:0000269|PubMed:8639592 |
| Chain | Residue | Details |
| K | ASN145 | |
| A | HIS654 | |
| A | HIS758 | |
| A | ASN139 | |
| A | SER269 | |
| A | ASP286 | |
| A | ASP288 | |
| A | GLU516 | |
| A | SER519 | |
| A | GLU546 | |
| A | ASP547 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19017259, ECO:0000269|PubMed:8639592 |
| Chain | Residue | Details |
| K | ASN195 | |
| A | LYS601 | |
| A | LYS648 | |
| A | LYS765 | |
| A | LYS776 | |
| A | LYS793 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | CARBOHYD: O-linked (GalNAc...) serine; partial => ECO:0000269|PubMed:19017259, ECO:0000269|PubMed:8639592 |
| Chain | Residue | Details |
| K | SER202 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | CARBOHYD: O-linked (GalNAc...) threonine => ECO:0000269|PubMed:19017259, ECO:0000269|PubMed:8639592 |
| Chain | Residue | Details |
| K | THR203 |
