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STRUCTURAL IMPLICATIONS OF DRUG RESISTANT MUTANTS OF HIV-1 PROTEASE : HIGH RESOLUTION CRYSTAL STRUCTURES OF THE MUTANT PROTEASE/SUBSTRATE ANALOG COMPLEXES.

Functional Information from GO Data
ChainGOidnamespacecontents
C0004190molecular_functionaspartic-type endopeptidase activity
C0006508biological_processproteolysis
D0004190molecular_functionaspartic-type endopeptidase activity
D0006508biological_processproteolysis
Functional Information from PDB Data
site_idAC1
Number of Residues28
DetailsBINDING SITE FOR RESIDUE 0Q4 D 401
ChainResidue
CTRP6
CGLY49
CILE84
DHOH7
DHOH77
DLEU123
DASP125
DGLY127
DALA128
DASP129
DASN130
CARG8
DMET146
DILE147
DGLY148
DGLY149
DILE150
DGLN158
DHOH201
DHOH207
DHOH249
CASP25
CGLY27
CALA28
CASP29
CASN30
CVAL32
CGLY48

Functional Information from PROSITE/UniProt
site_idPS00141
Number of Residues12
DetailsASP_PROTEASE Eukaryotic and viral aspartyl proteases active site. ALLDTGADNTVI
ChainResidueDetails
CALA22-ILE33

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsSITE: Cleavage; by viral protease => ECO:0000250
ChainResidueDetails
CILE64
DILE164

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: Phosphotyrosine; by host => ECO:0000250
ChainResidueDetails
CILE64
DILE164

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1a30
ChainResidueDetails
DTHR126
DASP125
CASP25
CTHR26

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1a30
ChainResidueDetails
CASP25
DASP125

229183

PDB entries from 2024-12-18

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