2PBH
CRYSTAL STRUCTURE OF HUMAN PROCATHEPSIN B AT 3.3 ANGSTROM RESOLUTION
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004175 | molecular_function | endopeptidase activity |
A | 0004197 | molecular_function | cysteine-type endopeptidase activity |
A | 0005515 | molecular_function | protein binding |
A | 0005518 | molecular_function | collagen binding |
A | 0005576 | cellular_component | extracellular region |
A | 0005615 | cellular_component | extracellular space |
A | 0005764 | cellular_component | lysosome |
A | 0005886 | cellular_component | plasma membrane |
A | 0006508 | biological_process | proteolysis |
A | 0006590 | biological_process | thyroid hormone generation |
A | 0008233 | molecular_function | peptidase activity |
A | 0008234 | molecular_function | cysteine-type peptidase activity |
A | 0009897 | cellular_component | external side of plasma membrane |
A | 0016324 | cellular_component | apical plasma membrane |
A | 0030574 | biological_process | collagen catabolic process |
A | 0030855 | biological_process | epithelial cell differentiation |
A | 0036021 | cellular_component | endolysosome lumen |
A | 0042470 | cellular_component | melanosome |
A | 0042981 | biological_process | regulation of apoptotic process |
A | 0043394 | molecular_function | proteoglycan binding |
A | 0046697 | biological_process | decidualization |
A | 0046718 | biological_process | symbiont entry into host cell |
A | 0048471 | cellular_component | perinuclear region of cytoplasm |
A | 0050790 | biological_process | regulation of catalytic activity |
A | 0051603 | biological_process | proteolysis involved in protein catabolic process |
A | 0062023 | cellular_component | collagen-containing extracellular matrix |
A | 0070062 | cellular_component | extracellular exosome |
A | 0097067 | biological_process | cellular response to thyroid hormone stimulus |
A | 1904090 | cellular_component | peptidase inhibitor complex |
A | 1904813 | cellular_component | ficolin-1-rich granule lumen |
Functional Information from PROSITE/UniProt
site_id | PS00139 |
Number of Residues | 12 |
Details | THIOL_PROTEASE_CYS Eukaryotic thiol (cysteine) proteases cysteine active site. QGsCGSCWAfGA |
Chain | Residue | Details |
A | GLN23-ALA34 |
site_id | PS00639 |
Number of Residues | 11 |
Details | THIOL_PROTEASE_HIS Eukaryotic thiol (cysteine) proteases histidine active site. GGHAIRILGWG |
Chain | Residue | Details |
A | GLY197-GLY207 |
site_id | PS00640 |
Number of Residues | 20 |
Details | THIOL_PROTEASE_ASN Eukaryotic thiol (cysteine) proteases asparagine active site. YWLvANSWntdWGdnGFFkI |
Chain | Residue | Details |
A | TYR214-ILE233 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 3 |
Details | ACT_SITE: ACT_SITE => ECO:0000269|PubMed:9299326 |
Chain | Residue | Details |
A | GLY92 |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P10605 |
Chain | Residue | Details |
A | LEU204 |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:3463996 |
Chain | Residue | Details |
A | VAL176 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1pad |
Chain | Residue | Details |
A | HIS199 | |
A | ASN219 | |
A | CYS29 |
site_id | CSA2 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1pad |
Chain | Residue | Details |
A | HIS199 | |
A | GLN23 | |
A | CYS29 |
site_id | CSA3 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1pad |
Chain | Residue | Details |
A | HIS199 | |
A | ASN219 | |
A | GLN23 |