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6OPT

HIV-1 Protease NL4-3 V82F, I84V Mutant in complex with darunavir

Functional Information from GO Data
ChainGOidnamespacecontents
A0004190molecular_functionaspartic-type endopeptidase activity
A0006508biological_processproteolysis
A0008233molecular_functionpeptidase activity
A0016787molecular_functionhydrolase activity
A0055036cellular_componentvirion membrane
A0072494cellular_componenthost multivesicular body
B0004190molecular_functionaspartic-type endopeptidase activity
B0006508biological_processproteolysis
B0008233molecular_functionpeptidase activity
B0016787molecular_functionhydrolase activity
B0055036cellular_componentvirion membrane
B0072494cellular_componenthost multivesicular body
Functional Information from PDB Data
site_idAC1
Number of Residues18
Detailsbinding site for residue 017 A 101
ChainResidue
AASP25
BASP25
BGLY27
BALA28
BASP30
BVAL32
BGLY48
BGLY49
BPRO81
BPHE82
AGLY27
AALA28
AASP29
AASP30
AGLY48
AILE50
AHOH213
AHOH220

site_idAC2
Number of Residues6
Detailsbinding site for residue SO4 A 102
ChainResidue
AGLY68
AHIS69
ALYS70
AHOH203
AHOH222
BPRO1

site_idAC3
Number of Residues5
Detailsbinding site for residue SO4 A 103
ChainResidue
AMET36
AASN37
AHOH243
BPRO39
BGLY40

Functional Information from PROSITE/UniProt
site_idPS00141
Number of Residues12
DetailsASP_PROTEASE Eukaryotic and viral aspartyl proteases active site. ALLDTGADDTVL
ChainResidueDetails
BALA22-LEU33

246031

PDB entries from 2025-12-10

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