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1FQX

CRYSTAL STRUCTURE OF THE COMPLEX OF HIV-1 PROTEASE WITH A PEPTIDOMIMETIC INHIBITOR

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 Residues35
DetailsBINDING SITE FOR RESIDUE 0ZT A 201
ChainResidue
ALEU23
AGLY49
AILE50
APRO81
AVAL82
AILE84
AHOH301
AHOH305
AHOH307
AHOH313
AHOH314
AASP25
AHOH314
AHOH325
BLEU23
BASP25
BGLY27
BALA28
BASP29
BASP30
BVAL32
BILE47
AGLY27
BGLY48
BGLY49
BILE50
BPRO81
BVAL82
BILE84
AALA28
AASP29
AASP30
AVAL32
AILE47
AGLY48

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

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsSITE: Cleavage; by viral protease => ECO:0000250
ChainResidueDetails
AILE64
BILE64

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: Phosphotyrosine; by host => ECO:0000250
ChainResidueDetails
AILE64
BILE64

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1a30
ChainResidueDetails
AASP25
ATHR26
BASP25
BTHR26

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1a30
ChainResidueDetails
AASP25
BASP25

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PDB entries from 2024-10-30

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