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5AH8

Disubstituted bis-THF moieties as new P2 ligands in non-peptidal HIV- 1 Protease Inhibitors (II)

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 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
BHOH2111

site_idAC4
Number of Residues21
DetailsBINDING SITE FOR RESIDUE C7W A 1101
ChainResidue
AGLY27
AALA28
AASP29
AASP30
AGLY48
AGLY49
AILE50
APHE53
AHOH2093
AHOH2154
BASP125
BGLY127
BALA128
BASP130
BILE147
BGLY148
BGLY149
BPRO181
BTHR182
ATRP6
AASP25

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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