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7M9O

HIV-1 Protease (I84V) in Complex with LR3-48

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 Residues6
Detailsbinding site for residue SO4 B 101
ChainResidue
AGLY68
AHIS69
ALYS70
AHOH229
BPRO1
BLYS55

site_idAC2
Number of Residues5
Detailsbinding site for residue SO4 B 102
ChainResidue
BGLN92
BHOH213
BGLY73
BTHR74
BASN88

site_idAC3
Number of Residues6
Detailsbinding site for residue SO4 B 103
ChainResidue
ALYS14
BLYS14
BILE15
BGLY16
BGLY17
BHOH207

site_idAC4
Number of Residues4
Detailsbinding site for residue SO4 A 101
ChainResidue
AMET36
AASN37
BPRO39
BGLY40

site_idAC5
Number of Residues4
Detailsbinding site for residue SO4 A 102
ChainResidue
ALYS7
AARG8
AHOH232
AHOH243

site_idAC6
Number of Residues1
Detailsbinding site for residue SO4 A 103
ChainResidue
AGLN58

site_idAC7
Number of Residues24
Detailsbinding site for residue YWP A 104
ChainResidue
AASP25
AGLY27
AALA28
AASP29
AASP30
AGLY48
AGLY49
AILE50
APHE53
AVAL82
AHOH204
BARG8
BASP25
BGLY27
BALA28
BASP29
BASP30
BVAL32
BGLY48
BGLY49
BLEU76
BPRO81
BHOH206
BHOH242

Functional Information from PROSITE/UniProt
site_idPS00141
Number of Residues12
DetailsASP_PROTEASE Eukaryotic and viral aspartyl proteases active site. ALLDTGADDTVL
ChainResidueDetails
BALA22-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
BASP25
AASP25

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

222624

PDB entries from 2024-07-17

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