Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004190 | molecular_function | aspartic-type endopeptidase activity |
| A | 0006508 | biological_process | proteolysis |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL A 201 |
| Chain | Residue |
| A | LYS120 |
| A | GLU121 |
| A | GLU134 |
| A | ASN183 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE PO4 A 202 |
| Chain | Residue |
| A | HOH315 |
| A | HOH354 |
| A | GLY16 |
| A | PRO63 |
| A | GLY116 |
| A | GLY117 |
| A | HOH304 |
| site_id | AC3 |
| Number of Residues | 29 |
| Details | BINDING SITE FOR CHAIN B OF SUBSTRATE RT-RH |
| Chain | Residue |
| A | ARG8 |
| A | ASN25 |
| A | GLY27 |
| A | ALA28 |
| A | ASP29 |
| A | ASP30 |
| A | ILE47 |
| A | GLY48 |
| A | GLY49 |
| A | ILE50 |
| A | PRO81 |
| A | VAL82 |
| A | ARG108 |
| A | LEU123 |
| A | ASN125 |
| A | GLY127 |
| A | ALA128 |
| A | ASP129 |
| A | ASP130 |
| A | ILE147 |
| A | GLY148 |
| A | GLY149 |
| A | ILE150 |
| A | PRO181 |
| A | VAL182 |
| A | ILE184 |
| B | HOH101 |
| B | HOH102 |
| B | HOH103 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 69 |
| Details | Domain: {"description":"Peptidase A2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00275","evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 10 |
| Details | Region: {"description":"Dimerization of protease","evidences":[{"source":"UniProtKB","id":"P04585","evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Active site: {"description":"For protease activity; shared with dimeric partner","evidences":[{"source":"PROSITE-ProRule","id":"PRU10094","evidenceCode":"ECO:0000255"}]} |
