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3KFR

HIV Protease (PR) dimer with inhibitor TL-3 bound and fragment 1F1 in the outside/top of flap

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 3TL A 200
ChainResidue
AARG8
AGLY49
AILE50
APRO79
APRO81
AVAL82
AILE84
AHOH263
AHOH283
BASP25
BGLY27
AASP25
BALA28
BASP29
BASP30
BGLY48
BGLY49
BILE50
BPHE53
BVAL82
BILE84
AGLY27
AALA28
AASP29
APRO44
AMET46
AILE47
AGLY48

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE BME A 202
ChainResidue
AVAL11
ATHR12
ACYS67
AHOH287
AHOH356
BLYS7

site_idAC3
Number of Residues11
DetailsBINDING SITE FOR RESIDUE 1F1 B 201
ChainResidue
BPRO44
BLYS45
BLYS55
BVAL56
BARG57
BTHR91
BGLN92
BGLY94
BHOH210
BHOH310
BHOH333

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE BME B 203
ChainResidue
ALYS7
BVAL11
BTHR12
BCYS67
BHOH222
BHOH311

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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