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6UWB

X-ray crystal structure of wild type HIV-1 protease in complex with GRL-08513

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 Residues25
Detailsbinding site for residue QJY A 400
ChainResidue
AARG8
APRO81
AVAL82
AILE84
AHOH504
BARG8
BASP25
BGLY27
BALA28
BASP29
BASP30
AASP25
BGLY48
BGLY49
BILE50
BPRO81
BVAL82
BILE84
AGLY27
AALA28
AASP29
AASP30
AGLY48
AGLY49
AILE50

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
ChainResidueDetails
AASP25
BASP25

site_idSWS_FT_FI2
Number of Residues2
DetailsSITE: Cleavage; by viral protease => ECO:0000250
ChainResidueDetails
APHE99
BPHE99

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PDB entries from 2024-07-31

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