2NQD
Crystal structure of cysteine protease inhibitor, chagasin, in complex with human cathepsin L
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004869 | molecular_function | cysteine-type endopeptidase inhibitor activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0009986 | cellular_component | cell surface |
| A | 0020016 | cellular_component | ciliary pocket |
| A | 0030414 | molecular_function | peptidase inhibitor activity |
| A | 0031410 | cellular_component | cytoplasmic vesicle |
| B | 0006508 | biological_process | proteolysis |
| B | 0008234 | molecular_function | cysteine-type peptidase activity |
Functional Information from PROSITE/UniProt
| site_id | PS00639 |
| Number of Residues | 11 |
| Details | THIOL_PROTEASE_HIS Eukaryotic thiol (cysteine) proteases histidine active site. MDHGVLVVGYG |
| Chain | Residue | Details |
| B | MET161-GLY171 |
| site_id | PS00640 |
| Number of Residues | 20 |
| Details | THIOL_PROTEASE_ASN Eukaryotic thiol (cysteine) proteases asparagine active site. YWLvKNSWgeeWGmgGYVkM |
| Chain | Residue | Details |
| B | TYR182-MET201 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 5 |
| Details | Motif: {"description":"BC loop","evidences":[{"source":"PubMed","id":"17502099","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17561110","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18515357","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19143838","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 9 |
| Details | Motif: {"description":"DE loop","evidences":[{"source":"PubMed","id":"17502099","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17561110","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18515357","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19143838","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 9 |
| Details | Motif: {"description":"FG loop","evidences":[{"source":"PubMed","id":"17502099","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17561110","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18515357","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19143838","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Propeptide: {"featureId":"PRO_0000026246"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | Active site: {"evidences":[{"source":"PubMed","id":"9468501","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | Active site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 11 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"37990007","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"8HFV","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 1 |
| Details | Site: {"description":"Cleavage; by autolysis","evidences":[{"source":"PubMed","id":"9468501","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 1 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"12754519","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 9pap |
| Chain | Residue | Details |
| B | ASN187 | |
| B | GLN19 | |
| B | HIS163 |
