8PRX
Crystal structure of human cathepsin L after reaction with the bound ketoamide inhibitor 13b
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0006508 | biological_process | proteolysis |
A | 0008234 | molecular_function | cysteine-type peptidase activity |
B | 0006508 | biological_process | proteolysis |
B | 0008234 | molecular_function | cysteine-type peptidase activity |
C | 0006508 | biological_process | proteolysis |
C | 0008234 | molecular_function | cysteine-type peptidase activity |
D | 0006508 | biological_process | proteolysis |
D | 0008234 | molecular_function | cysteine-type peptidase activity |
Functional Information from PROSITE/UniProt
site_id | PS00139 |
Number of Residues | 12 |
Details | THIOL_PROTEASE_CYS Eukaryotic thiol (cysteine) proteases cysteine active site. QGqCGSCWAfSA |
Chain | Residue | Details |
A | GLN19-ALA30 |
site_id | PS00639 |
Number of Residues | 11 |
Details | THIOL_PROTEASE_HIS Eukaryotic thiol (cysteine) proteases histidine active site. MDHGVLVVGYG |
Chain | Residue | Details |
A | MET161-GLY171 |
site_id | PS00640 |
Number of Residues | 20 |
Details | THIOL_PROTEASE_ASN Eukaryotic thiol (cysteine) proteases asparagine active site. YWLvKNSWgeeWGmgGYVkM |
Chain | Residue | Details |
A | TYR182-MET201 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 6 |
Details | Propeptide: {"featureId":"PRO_0000026246"} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | Active site: {"evidences":[{"source":"PubMed","id":"9468501","evidenceCode":"ECO:0000305"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 8 |
Details | Active site: {} |
Chain | Residue | Details |
site_id | SWS_FT_FI4 |
Number of Residues | 44 |
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_FI5 |
Number of Residues | 4 |
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 |