Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0006508 | biological_process | proteolysis |
| A | 0008234 | molecular_function | cysteine-type peptidase activity |
| I | 0004869 | molecular_function | cysteine-type endopeptidase inhibitor activity |
| I | 0005515 | molecular_function | protein binding |
| I | 0005576 | cellular_component | extracellular region |
| I | 0005615 | cellular_component | extracellular space |
| I | 0005737 | cellular_component | cytoplasm |
| I | 0030414 | molecular_function | peptidase inhibitor activity |
| I | 0031982 | cellular_component | vesicle |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL A 1001 |
| Chain | Residue |
| A | ASP114 |
| A | ASN115 |
| I | THR70 |
| I | HIS84 |
| I | ASP85 |
| I | GLU86 |
| I | MET89 |
Functional Information from PROSITE/UniProt
| site_id | PS00139 |
| Number of Residues | 12 |
| Details | THIOL_PROTEASE_CYS Eukaryotic thiol (cysteine) proteases cysteine active site. QKnCGSCWAfSS |
| Chain | Residue | Details |
| A | GLN19-SER30 | |
| site_id | PS00287 |
| Number of Residues | 14 |
| Details | CYSTATIN Cysteine proteases inhibitors signature. RQLVSGIKYiLQVE |
| Chain | Residue | Details |
| I | ARG52-GLU65 | |
| site_id | PS00639 |
| Number of Residues | 11 |
| Details | THIOL_PROTEASE_HIS Eukaryotic thiol (cysteine) proteases histidine active site. LNHAVMLVGFG |
| Chain | Residue | Details |
| A | LEU157-GLY167 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 16 |
| Details | Motif: {"description":"Nose motif; required for the correct folding of the mature form","evidences":[{"source":"PubMed","id":"11827964","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 9 |
| Details | Motif: {"description":"Arm motif; binds to host hemoglobin and required for the inhibitory interaction between the propeptide and the catalytic domain","evidences":[{"source":"PubMed","id":"15964982","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Active site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU10088","evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Active site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU10089","evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | Active site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU10090","evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI7 |
| Number of Residues | 4 |
| Details | Motif: {"description":"Secondary area of contact"} |
| site_id | SWS_FT_FI8 |
| Number of Residues | 1 |
| Details | Site: {"description":"Reactive site"} |
| site_id | SWS_FT_FI9 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"2721673","evidenceCode":"ECO:0000269"}]} |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1pad |
| Chain | Residue | Details |
| A | ASN175 | |
| A | CYS25 | |
| A | HIS159 | |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1pad |
| Chain | Residue | Details |
| A | GLN19 | |
| A | CYS25 | |
| A | HIS159 | |
| site_id | CSA3 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1pad |
| Chain | Residue | Details |
| A | ASN175 | |
| A | GLN19 | |
| A | HIS159 | |
