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4COE

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 Residues1
DetailsBINDING SITE FOR RESIDUE CL B 1200
ChainResidue
BTRP106

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL A 1100
ChainResidue
AGLY73
ATHR74
AASN88
BARG141

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL B 1201
ChainResidue
BTHR174
BASN188
BHOH2106

site_idAC4
Number of Residues27
DetailsBINDING SITE FOR RESIDUE M17 A 1101
ChainResidue
AASP25
AGLY27
AALA28
AASP29
AASP30
AGLY48
AGLY49
AILE50
APRO81
ATHR82
AHOH2043
AHOH2047
AHOH2075
AHOH2093
AHOH2153
AHOH2154
BARG108
BASP125
BGLY127
BALA128
BASP129
BGLY148
BGLY149
BPHE153
BTHR182
BHOH2079
AARG8

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

222415

PDB entries from 2024-07-10

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