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2Q5K

Crystal structure of lopinavir bound to wild type HIV-1 protease

Functional Information from GO Data
ChainGOidnamespacecontents
A0004190molecular_functionaspartic-type endopeptidase activity
A0006508biological_processproteolysis
A0008233molecular_functionpeptidase activity
A0016787molecular_functionhydrolase activity
B0004190molecular_functionaspartic-type endopeptidase activity
B0006508biological_processproteolysis
B0008233molecular_functionpeptidase activity
B0016787molecular_functionhydrolase activity
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PO4 B 202
ChainResidue
BLYS20
BGLU21
BASN83
BHOH215

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE PO4 A 203
ChainResidue
ALYS7
AARG8
AHOH256

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE PO4 A 204
ChainResidue
BPRO1
AHIS69
ALYS70

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE PO4 A 205
ChainResidue
AGLY40
ACYS67
AHOH214

site_idAC5
Number of Residues18
DetailsBINDING SITE FOR RESIDUE AB1 A 201
ChainResidue
AASP25
AGLY27
AALA28
AASP29
AGLY48
AGLY49
AHOH223
BARG8
BASP25
BGLY27
BALA28
BASP29
BASP30
BVAL32
BGLY48
BGLY49
BILE50
BVAL82

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

218853

PDB entries from 2024-04-24

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