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4HDF

Crystal Structure of HIV-1 protease mutants V82A complexed with inhibitor GRL-0519

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 Residues26
DetailsBINDING SITE FOR RESIDUE G52 A 401
ChainResidue
AARG8
AILE84
AHOH519
AHOH563
AHOH565
AHOH587
BARG8
BLEU23
BASP25
BGLY27
BALA28
AASP25
BASP29
BASP30
BGLY48
BGLY49
BILE50
BALA82
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. ALLDTGADDTVI
ChainResidueDetails
BALA22-ILE33

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
BASP25
AASP25

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

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PDB entries from 2024-07-17

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