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 |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE PO4 A 501 |
Chain | Residue |
A | ARG14 |
B | HOH521 |
A | GLY16 |
A | GLY17 |
A | PRO63 |
A | HOH523 |
A | HOH530 |
A | HOH593 |
A | HOH594 |
B | ARG14 |
site_id | AC2 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE PO4 A 502 |
Chain | Residue |
A | GLY73 |
A | THR74 |
A | ASN88 |
A | GLN92 |
A | HOH513 |
A | HOH515 |
A | HOH537 |
A | HOH560 |
site_id | AC3 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE PO4 A 503 |
Chain | Residue |
A | PRO1 |
A | LYS55 |
B | HIS69 |
B | LYS70 |
B | PHE99 |
B | HOH550 |
B | HOH574 |
B | HOH589 |
site_id | AC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE PO4 B 504 |
Chain | Residue |
A | ARG14 |
A | LYS70 |
B | LYS55 |
B | LYS70 |
site_id | AC5 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE PO4 B 505 |
Chain | Residue |
A | QNC508 |
B | ARG8 |
B | HOH587 |
site_id | AC6 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE PO4 B 506 |
Chain | Residue |
A | HOH568 |
B | PRO1 |
B | ARG57 |
B | HIS69 |
B | HOH555 |
site_id | AC7 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE PO4 A 507 |
Chain | Residue |
A | LYS7 |
A | ARG8 |
A | HOH572 |
A | HOH589 |
B | ARG87 |
site_id | AC8 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE QNC A 508 |
Chain | Residue |
A | GLY27 |
A | ASP29 |
A | GLY48 |
A | ASN509 |
A | HPH510 |
A | HOH531 |
B | ARG8 |
B | PRO81 |
B | PO4505 |
site_id | AC9 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE ASN A 509 |
Chain | Residue |
A | ALA28 |
A | ASP29 |
A | ASP30 |
A | GLY48 |
A | GLY49 |
A | QNC508 |
A | HPH510 |
A | HOH526 |
A | HOH534 |
B | ILE50 |
site_id | BC1 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE HPH A 510 |
Chain | Residue |
A | ASP25 |
A | GLY27 |
A | GLY49 |
A | ILE50 |
A | QNC508 |
A | ASN509 |
A | DIQ511 |
B | ASP25 |
B | VAL82 |
B | ILE84 |
site_id | BC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE DIQ A 511 |
Chain | Residue |
A | ASP25 |
A | HPH510 |
A | NTB512 |
A | HOH526 |
B | ASP25 |
B | GLY49 |
site_id | BC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE NTB A 512 |
Chain | Residue |
A | ILE50 |
A | DIQ511 |
B | GLY48 |
B | HOH508 |
Functional Information from PROSITE/UniProt
site_id | PS00141 |
Number of Residues | 12 |
Details | ASP_PROTEASE Eukaryotic and viral aspartyl proteases active site. ALLDTGADDTVL |
Chain | Residue | Details |
A | ALA22-LEU33 | |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
A | ASP25 | |
B | ASP25 | |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | SITE: Cleavage; by viral protease => ECO:0000250 |
Chain | Residue | Details |
A | PHE99 | |
B | PHE99 | |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1a30 |
Chain | Residue | Details |
A | ASP25 | |
A | THR26 | |
B | ASP25 | |
B | THR26 | |
site_id | CSA2 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1a30 |
Chain | Residue | Details |
A | ASP25 | |
B | ASP25 | |