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7LE7

HIV-1 Protease WT (NL4-3) in Complex with GS-8374

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 Residues5
Detailsbinding site for residue SO4 B 101
ChainResidue
BLYS20
BGLU21
BASN83
BHOH203
BHOH248

site_idAC2
Number of Residues2
Detailsbinding site for residue SO4 A 101
ChainResidue
AARG8
AHOH221

site_idAC3
Number of Residues5
Detailsbinding site for residue SO4 A 102
ChainResidue
ALYS70
AHOH204
BPRO1
AGLY68
AHIS69

site_idAC4
Number of Residues6
Detailsbinding site for residue SO4 A 103
ChainResidue
AGLN18
AMET36
AASN37
AHOH208
BPRO39
BGLY40

site_idAC5
Number of Residues23
Detailsbinding site for residue KGQ A 104
ChainResidue
AASP25
AGLY27
AALA28
AASP29
AASP30
AGLY48
AGLY49
AILE50
APHE53
AVAL82
AHOH201
AHOH214
AHOH223
BASP25
BGLY27
BALA28
BASP30
BILE47
BGLY48
BGLY49
BPRO81
BGLN92
BHOH246

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

219869

PDB entries from 2024-05-15

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