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4CPR

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 1200
ChainResidue
BTRP106
BHOH2089

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL A 1100
ChainResidue
ATHR74
AASN88
BARG141

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL B 1201
ChainResidue
BTHR174
BASN188
BHOH2105

site_idAC4
Number of Residues28
DetailsBINDING SITE FOR RESIDUE 378 A 1101
ChainResidue
AASP25
AGLY27
AALA28
AASP29
AASP30
AGLY48
AGLY49
AILE50
APRO81
ATHR82
AHOH2038
AHOH2069
AHOH2089
AHOH2090
AHOH2150
AHOH2151
BARG108
BLEU123
BASP125
BGLY127
BALA128
BASP129
BGLY148
BGLY149
BPHE153
BPRO181
BTHR182
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

222624

PDB entries from 2024-07-17

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