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2FLE

Structural analysis of asymmetric inhibitor bound to the HIV-1 Protease V82A mutant

Functional Information from GO Data
ChainGOidnamespacecontents
A0004190molecular_functionaspartic-type endopeptidase activity
A0006508biological_processproteolysis
A0008233molecular_functionpeptidase activity
A0016787molecular_functionhydrolase activity
A0044174cellular_componenthost cell endosome
A0055036cellular_componentvirion membrane
A0072494cellular_componenthost multivesicular body
B0004190molecular_functionaspartic-type endopeptidase activity
B0006508biological_processproteolysis
B0008233molecular_functionpeptidase activity
B0016787molecular_functionhydrolase activity
B0044174cellular_componenthost cell endosome
B0055036cellular_componentvirion membrane
B0072494cellular_componenthost multivesicular body
Functional Information from PDB Data
site_idAC1
Number of Residues25
DetailsBINDING SITE FOR RESIDUE AI B 845
ChainResidue
AARG8
AILE50
AALA82
AILE84
BARG8
BLEU23
BASP25
BGLY27
BALA28
BASP29
BILE47
ALEU23
BGLY48
BGLY49
BILE50
BALA82
BILE84
BHOH846
AASP25
AGLY27
AALA28
AASP29
AILE47
AGLY48
AGLY49

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL A 300
ChainResidue
AASP29
AARG87
AASN88
AHOH330
BTRP6

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

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1a30
ChainResidueDetails
AASP25
ATHR26
BASP25
BTHR26

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1a30
ChainResidueDetails
AASP25
BASP25

237992

PDB entries from 2025-06-25

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