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4LL3

Structure of wild-type HIV protease in complex with darunavir

Replaces:  3QOZ
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 Residues21
DetailsBINDING SITE FOR RESIDUE 017 A 201
ChainResidue
AASP25
AHOH301
AHOH359
BLEU23
BASP25
BGLY27
BALA28
BASP29
BASP30
BGLY48
BGLY49
AGLY27
BILE50
BILE84
AALA28
AASP30
AVAL32
AGLY48
AGLY49
APRO81
AILE84

site_idAC2
Number of Residues22
DetailsBINDING SITE FOR RESIDUE 017 A 202
ChainResidue
AASP25
AGLY27
AALA28
AASP29
AASP30
AGLY48
AGLY49
AILE50
AILE84
AHOH301
AHOH358
BASP25
BGLY27
BALA28
BASP30
BVAL32
BGLY48
BGLY49
BPRO81
BVAL82
BILE84
BHOH163

Functional Information from PROSITE/UniProt
site_idPS00141
Number of Residues12
DetailsASP_PROTEASE Eukaryotic and viral aspartyl proteases active site. ALLDTGADDTVL
ChainResidueDetails
AALA22-LEU33

226262

PDB entries from 2024-10-16

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