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3T11

Dimeric inhibitor of HIV-1 protease.

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 Residues15
DetailsBINDING SITE FOR RESIDUE 3T1 A 101
ChainResidue
AGLY27
AHOH217
AHOH225
BARG8
BPRO81
BVAL82
B3T1101
AALA28
AVAL32
AILE47
AGLY48
APRO79
ATHR80
ACL102
AHOH201

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CL A 102
ChainResidue
AGLY49
AILE50
A3T1101
BGLY49
BILE50
B3T1101

site_idAC3
Number of Residues1
DetailsBINDING SITE FOR RESIDUE BME A 103
ChainResidue
ACYS67

site_idAC4
Number of Residues16
DetailsBINDING SITE FOR RESIDUE 3T1 B 101
ChainResidue
AARG8
ALEU23
AILE50
APRO81
AVAL82
A3T1101
ACL102
BTHR4
BGLY27
BALA28
BILE47
BGLY48
BTHR80
BHOH205
BHOH207
BHOH220

site_idAC5
Number of Residues1
DetailsBINDING SITE FOR RESIDUE BME B 102
ChainResidue
BCYS67

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
ChainResidueDetails
AASP25
BASP25

site_idSWS_FT_FI2
Number of Residues2
DetailsSITE: Cleavage; by viral protease => ECO:0000250
ChainResidueDetails
APHE99
BPHE99

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PDB entries from 2024-06-12

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