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2RKG

HIV-1 PR resistant mutant + LPV

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 Residues25
DetailsBINDING SITE FOR RESIDUE AB1 B 501
ChainResidue
AASP25
AHOH1005
AHOH1064
BASP25
BGLY27
BALA28
BASP29
BASP30
BGLY49
BGLY50
BILE51
AGLY27
BPRO82
BHOH1006
BHOH1010
BHOH1063
BHOH1064
BHOH1077
AALA28
AASP29
AASP30
AGLY49
AGLY50
AILE51
APRO82

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL B 1001
ChainResidue
ATRP6
BASP29
BARG88
BASN89

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL A 1002
ChainResidue
AASP29
AARG88
AASN89
BTRP6

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

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1a30
ChainResidueDetails
AASP25
ATHR26

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1a30
ChainResidueDetails
BASP25
BTHR26

site_idCSA3
Number of Residues1
DetailsAnnotated By Reference To The Literature 1a30
ChainResidueDetails
AASP25

site_idCSA4
Number of Residues1
DetailsAnnotated By Reference To The Literature 1a30
ChainResidueDetails
BASP25

249697

PDB entries from 2026-02-25

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