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7M9Q

HIV-1 Protease WT (NL4-3) in Complex with LR4-33

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
BLYS7
BARG8
BHOH205
BHOH216
BHOH220

site_idAC2
Number of Residues24
Detailsbinding site for residue YUM A 101
ChainResidue
AASP29
AASP30
AGLY48
AGLY49
AILE50
AHOH228
BASP25
BGLY27
BALA28
BASP29
BASP30
BVAL32
BILE47
BGLY48
BGLY49
BPRO81
BVAL82
BILE84
BHOH202
BHOH234
ATRP6
AASP25
AGLY27
AALA28

site_idAC3
Number of Residues3
Detailsbinding site for residue SO4 A 102
ChainResidue
ALYS7
AARG8
BHOH232

site_idAC4
Number of Residues4
Detailsbinding site for residue SO4 A 103
ChainResidue
ALYS20
AGLU21
AASN83
AHOH202

site_idAC5
Number of Residues5
Detailsbinding site for residue SO4 A 104
ChainResidue
AMET36
AASN37
BPRO39
BGLY40
BHOH210

site_idAC6
Number of Residues1
Detailsbinding site for residue SO4 A 105
ChainResidue
AARG8

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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