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3KFS

HIV Protease (PR) dimer with inhibitor TL-3 bound and fragment 2F4 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 Residues22
DetailsBINDING SITE FOR RESIDUE 3TL A 200
ChainResidue
AARG8
AILE50
APRO81
AHOH265
BASP25
BGLY27
BALA28
BASP29
BASP30
BGLY48
BGLY49
AASP25
BILE50
BVAL82
BILE84
AGLY27
AALA28
AASP29
AMET46
AILE47
AGLY48
AGLY49

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE DMS A 302
ChainResidue
ALYS14
AILE15
AGLY16
AGLY17
ALEU63
AILE64
AGLU65

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE DMS A 304
ChainResidue
ATRP6
BLEU19
BARG87
BASN88
BHOH278

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE BME A 401
ChainResidue
AVAL11
ATHR12
ACYS67
BLYS7
BHOH254

site_idAC5
Number of Residues9
DetailsBINDING SITE FOR RESIDUE 2FX B 201
ChainResidue
ATRP6
BPRO44
BLYS45
BLYS55
BVAL56
BGLN92
BILE93
BGLY94
BHOH208

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE DMS B 305
ChainResidue
BGLY73
BTHR74
BASN88
BGLN92

site_idAC7
Number of Residues3
DetailsBINDING SITE FOR RESIDUE BME B 402
ChainResidue
BVAL11
BTHR12
BCYS67

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

222036

PDB entries from 2024-07-03

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