1CQD
THE 2.1 ANGSTROM STRUCTURE OF A CYSTEINE PROTEASE WITH PROLINE SPECIFICITY FROM GINGER RHIZOME, ZINGIBER OFFICINALE
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004197 | molecular_function | cysteine-type endopeptidase activity |
| A | 0005615 | cellular_component | extracellular space |
| A | 0005764 | cellular_component | lysosome |
| A | 0006508 | biological_process | proteolysis |
| A | 0008234 | molecular_function | cysteine-type peptidase activity |
| A | 0051603 | biological_process | proteolysis involved in protein catabolic process |
| B | 0004197 | molecular_function | cysteine-type endopeptidase activity |
| B | 0005615 | cellular_component | extracellular space |
| B | 0005764 | cellular_component | lysosome |
| B | 0006508 | biological_process | proteolysis |
| B | 0008234 | molecular_function | cysteine-type peptidase activity |
| B | 0051603 | biological_process | proteolysis involved in protein catabolic process |
| C | 0004197 | molecular_function | cysteine-type endopeptidase activity |
| C | 0005615 | cellular_component | extracellular space |
| C | 0005764 | cellular_component | lysosome |
| C | 0006508 | biological_process | proteolysis |
| C | 0008234 | molecular_function | cysteine-type peptidase activity |
| C | 0051603 | biological_process | proteolysis involved in protein catabolic process |
| D | 0004197 | molecular_function | cysteine-type endopeptidase activity |
| D | 0005615 | cellular_component | extracellular space |
| D | 0005764 | cellular_component | lysosome |
| D | 0006508 | biological_process | proteolysis |
| D | 0008234 | molecular_function | cysteine-type peptidase activity |
| D | 0051603 | biological_process | proteolysis involved in protein catabolic process |
Functional Information from PDB Data
| site_id | CAA |
| Number of Residues | 2 |
| Details | CYS 27 AND HIS 161 ARE THE CATALYTIC DIAD. |
| Chain | Residue |
| A | CYS27 |
| A | HIS161 |
| site_id | CAB |
| Number of Residues | 2 |
| Details | CYS 27 AND HIS 161 ARE THE CATALYTIC DIAD. |
| Chain | Residue |
| B | CYS27 |
| B | HIS161 |
| site_id | CAC |
| Number of Residues | 2 |
| Details | CYS 27 AND HIS 161 ARE THE CATALYTIC DIAD. |
| Chain | Residue |
| C | CYS27 |
| C | HIS161 |
| site_id | CAD |
| Number of Residues | 2 |
| Details | CYS 27 AND HIS 161 ARE THE CATALYTIC DIAD. |
| Chain | Residue |
| D | CYS27 |
| D | HIS161 |
Functional Information from PROSITE/UniProt
| site_id | PS00139 |
| Number of Residues | 12 |
| Details | THIOL_PROTEASE_CYS Eukaryotic thiol (cysteine) proteases cysteine active site. QGgCGSCWAfST |
| Chain | Residue | Details |
| A | GLN21-THR32 |
| site_id | PS00639 |
| Number of Residues | 11 |
| Details | THIOL_PROTEASE_HIS Eukaryotic thiol (cysteine) proteases histidine active site. ANHALTVVGYG |
| Chain | Residue | Details |
| A | ALA159-GLY169 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | ACT_SITE: ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10088 |
| Chain | Residue | Details |
| A | CYS27 | |
| B | CYS27 | |
| C | CYS27 | |
| D | CYS27 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | ACT_SITE: ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10089 |
| Chain | Residue | Details |
| A | HIS161 | |
| B | HIS161 | |
| C | HIS161 | |
| D | HIS161 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255|PROSITE-ProRule:PRU00498, ECO:0000269|PubMed:10512617 |
| Chain | Residue | Details |
| A | ASN99 | |
| A | ASN156 | |
| B | ASN99 | |
| B | ASN156 | |
| C | ASN99 | |
| C | ASN156 | |
| D | ASN99 | |
| D | ASN156 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1pad |
| Chain | Residue | Details |
| A | ASN181 | |
| A | HIS161 | |
| A | CYS27 |
| site_id | CSA10 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1pad |
| Chain | Residue | Details |
| B | ASN181 | |
| B | GLN21 | |
| B | HIS161 |
| site_id | CSA11 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1pad |
| Chain | Residue | Details |
| C | ASN181 | |
| C | GLN21 | |
| C | HIS161 |
| site_id | CSA12 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1pad |
| Chain | Residue | Details |
| D | ASN181 | |
| D | GLN21 | |
| D | HIS161 |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1pad |
| Chain | Residue | Details |
| B | ASN181 | |
| B | HIS161 | |
| B | CYS27 |
| site_id | CSA3 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1pad |
| Chain | Residue | Details |
| C | ASN181 | |
| C | HIS161 | |
| C | CYS27 |
| site_id | CSA4 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1pad |
| Chain | Residue | Details |
| D | ASN181 | |
| D | HIS161 | |
| D | CYS27 |
| site_id | CSA5 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1pad |
| Chain | Residue | Details |
| A | GLN21 | |
| A | HIS161 | |
| A | CYS27 |
| site_id | CSA6 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1pad |
| Chain | Residue | Details |
| B | GLN21 | |
| B | HIS161 | |
| B | CYS27 |
| site_id | CSA7 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1pad |
| Chain | Residue | Details |
| C | GLN21 | |
| C | HIS161 | |
| C | CYS27 |
| site_id | CSA8 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1pad |
| Chain | Residue | Details |
| D | GLN21 | |
| D | HIS161 | |
| D | CYS27 |
| site_id | CSA9 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1pad |
| Chain | Residue | Details |
| A | ASN181 | |
| A | GLN21 | |
| A | HIS161 |
