1B5F
NATIVE CARDOSIN A FROM CYNARA CARDUNCULUS L.
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004190 | molecular_function | aspartic-type endopeptidase activity |
| A | 0006508 | biological_process | proteolysis |
| B | 0004190 | molecular_function | aspartic-type endopeptidase activity |
| B | 0006508 | biological_process | proteolysis |
| C | 0004190 | molecular_function | aspartic-type endopeptidase activity |
| C | 0006508 | biological_process | proteolysis |
| D | 0004190 | molecular_function | aspartic-type endopeptidase activity |
| D | 0006508 | biological_process | proteolysis |
Functional Information from PDB Data
| site_id | 1 |
| Number of Residues | 2 |
| Details | ASPARTIC PROTEINASE CATALYTIC SITE WATER 1014 ASSOCIATED TO CHAIN A CATALYTIC SITE WATER 1035 ASSOCIATED TO CHAIN C CATALYTIC SITE |
| Chain | Residue |
| A | ASP32 |
| A | ASP215 |
| site_id | 2 |
| Number of Residues | 1 |
| Details | N-GLYCOSYLATION SITE ON CHAIN A, ASN67: (A1->3)-MAN405 | ASN67-NAG401-(B1->4)-NAG403-(B1->4)-MAN404 | (A1->3)FUC402 |
| Chain | Residue |
| A | ASN67 |
| site_id | 3 |
| Number of Residues | 1 |
| Details | N-GLYCOSYLATION SITE ON CHAIN B, ASN257: ASN257-NAG501-(B1->4)-NAG503-(B1->4)-MAN504 | (A1->3)-FUC502 |
| Chain | Residue |
| B | ASN257 |
| site_id | 4 |
| Number of Residues | 2 |
| Details | N-GLYCOSYLATION SITE ON CHAIN C, ASN67: (A1->3)-MAN405 | ASN67-NAG401-(B1->4)-NAG403-(B1->4)-MAN404 | | (A1->3)-FUC402 (A1->6)-MAN406 |
| Chain | Residue |
| C | ASP32 |
| C | ASP215 |
| site_id | 5 |
| Number of Residues | 1 |
| Details | N-GLYCOSYLATION SITE ON CHAIN D, ASN257: ASN257-NAG501-(B1->4)-NAG503-(B1->4)-MAN504 | (A1->3)-FUC502 |
| Chain | Residue |
| C | ASN67 |
| site_id | 6 |
| Number of Residues | 1 |
| Details |
| Chain | Residue |
| D | ASN257 |
Functional Information from PROSITE/UniProt
| site_id | PS00141 |
| Number of Residues | 12 |
| Details | ASP_PROTEASE Eukaryotic and viral aspartyl proteases active site. VIFDTGSSVLWV |
| Chain | Residue | Details |
| A | VAL29-VAL40 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | Motif: {"description":"RGD motif","evidences":[{"source":"PubMed","id":"16279943","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Active site: {"evidences":[{"source":"UniProtKB","id":"P42210","evidenceCode":"ECO:0000250"},{"source":"PROSITE-ProRule","id":"PRU10094","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PROSITE-ProRule","id":"PRU00415","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"10488111","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9057834","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | Motif: {"description":"KGE motif","evidences":[{"source":"PubMed","id":"16279943","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1am5 |
| Chain | Residue | Details |
| A | ASP215 | |
| A | SER35 | |
| A | THR218 | |
| A | ASP32 |
| site_id | CSA10 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1am5 |
| Chain | Residue | Details |
| C | ASP215 | |
| C | THR218 | |
| C | ASP32 | |
| C | THR33 |
| site_id | CSA11 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1am5 |
| Chain | Residue | Details |
| A | ASP215 | |
| A | ASP32 |
| site_id | CSA12 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1am5 |
| Chain | Residue | Details |
| C | ASP215 | |
| C | ASP32 |
| site_id | CSA2 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1am5 |
| Chain | Residue | Details |
| C | ASP215 | |
| C | SER35 | |
| C | THR218 | |
| C | ASP32 |
| site_id | CSA3 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1am5 |
| Chain | Residue | Details |
| A | ASP215 | |
| A | SER216 | |
| A | ASP32 | |
| A | THR33 |
| site_id | CSA4 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1am5 |
| Chain | Residue | Details |
| C | ASP215 | |
| C | SER216 | |
| C | ASP32 | |
| C | THR33 |
| site_id | CSA5 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1am5 |
| Chain | Residue | Details |
| A | ASP215 | |
| A | SER35 | |
| A | ASP32 |
| site_id | CSA6 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1am5 |
| Chain | Residue | Details |
| C | ASP215 | |
| C | SER35 | |
| C | ASP32 |
| site_id | CSA7 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1am5 |
| Chain | Residue | Details |
| A | ASP215 | |
| A | TYR75 | |
| A | SER35 | |
| A | ASP32 |
| site_id | CSA8 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1am5 |
| Chain | Residue | Details |
| C | ASP215 | |
| C | TYR75 | |
| C | SER35 | |
| C | ASP32 |
| site_id | CSA9 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1am5 |
| Chain | Residue | Details |
| A | ASP215 | |
| A | THR218 | |
| A | ASP32 | |
| A | THR33 |






