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4RVJ

Crystal structure of multidrug-resistant clinical isolate A02 HIV-1 protease in complex with amprenavir

Functional Information from GO Data
ChainGOidnamespacecontents
A0004190molecular_functionaspartic-type endopeptidase activity
A0006508biological_processproteolysis
B0004190molecular_functionaspartic-type endopeptidase activity
B0006508biological_processproteolysis
C0004190molecular_functionaspartic-type endopeptidase activity
C0006508biological_processproteolysis
D0004190molecular_functionaspartic-type endopeptidase activity
D0006508biological_processproteolysis
Functional Information from PDB Data
site_idAC1
Number of Residues20
DetailsBINDING SITE FOR RESIDUE 478 B 101
ChainResidue
AASP25
BASP25
BGLY27
BALA28
BASP29
BASP30
BVAL32
BGLY48
BGLY49
BILE50
BILE84
AGLY27
BHOH202
AALA28
AASP30
AGLY48
AGLY49
APRO81
ATHR82
AHOH150

site_idAC2
Number of Residues18
DetailsBINDING SITE FOR RESIDUE 478 D 101
ChainResidue
CASP25
CGLY27
CALA28
CASP30
CGLY48
CGLY49
CTHR82
DASP25
DGLY27
DALA28
DASP29
DASP30
DVAL32
DGLY48
DGLY49
DILE50
DILE84
DHOH201

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

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PDB entries from 2024-07-24

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