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6D0E

X-ray crystal structure of wild type HIV-1 protease in complex with GRL-084-13

Functional Information from GO Data
ChainGOidnamespacecontents
A0004190molecular_functionaspartic-type endopeptidase activity
A0006508biological_processproteolysis
B0004190molecular_functionaspartic-type endopeptidase activity
B0006508biological_processproteolysis
Functional Information from PDB Data
site_idAC1
Number of Residues28
Detailsbinding site for residue FQ1 B 500
ChainResidue
AARG8
AGLY49
AILE50
APRO81
AVAL82
AILE84
BARG8
BASP25
BGLY27
BALA28
BASP29
AASP25
BASP30
BILE47
BGLY48
BGLY49
BILE50
BPRO81
BVAL82
BILE84
BHOH601
AGLY27
AALA28
AASP29
AASP30
AVAL32
AILE47
AGLY48

Functional Information from PROSITE/UniProt
site_idPS00141
Number of Residues12
DetailsASP_PROTEASE Eukaryotic and viral aspartyl proteases active site. ALLDTGADDTVL
ChainResidueDetails
AALA22-LEU33

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: For protease activity; shared with dimeric partner => ECO:0000255|PROSITE-ProRule:PRU10094, ECO:0000269|PubMed:12924029
ChainResidueDetails
AASP25
BASP25

site_idSWS_FT_FI2
Number of Residues2
DetailsSITE: Cleavage; by viral protease => ECO:0000269|PubMed:2476069
ChainResidueDetails
APHE99
BPHE99

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PDB entries from 2024-07-17

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