1XXF
Crystal Structure of the FXIa Catalytic Domain in Complex with Ecotin Mutant (EcotinP)
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004252 | molecular_function | serine-type endopeptidase activity |
| A | 0006508 | biological_process | proteolysis |
| B | 0004252 | molecular_function | serine-type endopeptidase activity |
| B | 0006508 | biological_process | proteolysis |
| C | 0004867 | molecular_function | serine-type endopeptidase inhibitor activity |
| C | 0005515 | molecular_function | protein binding |
| C | 0006952 | biological_process | defense response |
| C | 0010466 | biological_process | negative regulation of peptidase activity |
| C | 0030288 | cellular_component | outer membrane-bounded periplasmic space |
| C | 0042597 | cellular_component | periplasmic space |
| C | 0042803 | molecular_function | protein homodimerization activity |
| D | 0004867 | molecular_function | serine-type endopeptidase inhibitor activity |
| D | 0005515 | molecular_function | protein binding |
| D | 0006952 | biological_process | defense response |
| D | 0010466 | biological_process | negative regulation of peptidase activity |
| D | 0030288 | cellular_component | outer membrane-bounded periplasmic space |
| D | 0042597 | cellular_component | periplasmic space |
| D | 0042803 | molecular_function | protein homodimerization activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE NA B 1001 |
| Chain | Residue |
| B | ILE160 |
| B | ALA183 |
| B | ASP189 |
| B | TYR228 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE NA B 1002 |
| Chain | Residue |
| B | TRP137 |
| B | THR139 |
| B | PRO198 |
| B | SER198 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | SITE: Reactive bond |
| Chain | Residue | Details |
| C | ARG84 | |
| D | ARG84 | |
| A | SER195 | |
| B | HIS57 | |
| B | ASP102 | |
| B | SER195 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | LYS170 | |
| B | LYS170 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | CARBOHYD: N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:25092234 |
| Chain | Residue | Details |
| A | ASN73 | |
| B | ASN73 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | CARBOHYD: N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:1998667, ECO:0000269|PubMed:25092234 |
| Chain | Residue | Details |
| A | ASN113 | |
| B | ASN113 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1a0j |
| Chain | Residue | Details |
| A | ASP102 | |
| A | SER195 | |
| A | HIS57 |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1a0j |
| Chain | Residue | Details |
| B | ASP102 | |
| B | SER195 | |
| B | HIS57 |
| site_id | CSA3 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1a0j |
| Chain | Residue | Details |
| A | ASP102 | |
| A | SER195 | |
| A | GLY193 | |
| A | HIS57 |
| site_id | CSA4 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1a0j |
| Chain | Residue | Details |
| B | ASP102 | |
| B | SER195 | |
| B | GLY193 | |
| B | HIS57 |
| site_id | CSA5 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1a0j |
| Chain | Residue | Details |
| A | ASP102 | |
| A | SER195 | |
| A | HIS57 | |
| A | GLY196 |
| site_id | CSA6 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1a0j |
| Chain | Residue | Details |
| B | ASP102 | |
| B | SER195 | |
| B | HIS57 | |
| B | GLY196 |
