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4CPQ

Macrocyclic Transition-State Mimicking HIV-1 Protease Inhibitors Encompassing a Tertiary Alcohol

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 Residues2
DetailsBINDING SITE FOR RESIDUE CL B 1201
ChainResidue
BTRP106
BHOH2093

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL A 1100
ChainResidue
ATHR74
AASN88
AHOH2124
BARG141

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL B 1200
ChainResidue
BTHR174
BASN188
BHOH2109

site_idAC4
Number of Residues21
DetailsBINDING SITE FOR RESIDUE 9MW A 1101
ChainResidue
AARG8
AASP25
AGLY27
AALA28
AASP29
AGLY48
AGLY49
APRO81
AHOH2089
AHOH2090
AHOH2147
AHOH2149
BLEU123
BASP125
BGLY127
BALA128
BASP129
BGLY148
BGLY149
BPHE153
BTHR182

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, ECO:0000269|PubMed:12924029
ChainResidueDetails
AASP25
BASP125

site_idSWS_FT_FI2
Number of Residues2
DetailsSITE: Cleavage; by viral protease => ECO:0000269|PubMed:2476069
ChainResidueDetails
APHE99
BPHE199

219140

PDB entries from 2024-05-01

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