6D0E
X-ray crystal structure of wild type HIV-1 protease in complex with GRL-084-13
Functional Information from GO Data
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 28 |
Details | binding site for residue FQ1 B 500 |
Chain | Residue |
A | ARG8 |
A | GLY49 |
A | ILE50 |
A | PRO81 |
A | VAL82 |
A | ILE84 |
B | ARG8 |
B | ASP25 |
B | GLY27 |
B | ALA28 |
B | ASP29 |
A | ASP25 |
B | ASP30 |
B | ILE47 |
B | GLY48 |
B | GLY49 |
B | ILE50 |
B | PRO81 |
B | VAL82 |
B | ILE84 |
B | HOH601 |
A | GLY27 |
A | ALA28 |
A | ASP29 |
A | ASP30 |
A | VAL32 |
A | ILE47 |
A | GLY48 |
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
site_id | SWS_FT_FI1 |
Number of Residues | 138 |
Details | Domain: {"description":"Peptidase A2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00275","evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 20 |
Details | Region: {"description":"Dimerization of protease","evidences":[{"source":"UniProtKB","id":"P04585","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | Active site: {"description":"For protease activity; shared with dimeric partner","evidences":[{"source":"PROSITE-ProRule","id":"PRU10094","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"12924029","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |