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1SGU

Comparing the Accumulation of Active Site and Non-active Site Mutations in the HIV-1 Protease

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 Residues21
DetailsBINDING SITE FOR RESIDUE MK1 B 2632
ChainResidue
AASP25
BASP25
BGLY27
BALA28
BASP29
BASP30
BILE47
BGLY48
BILE50
BPRO81
BHOH2633
AGLY27
BHOH2641
BHOH2674
AILE47
AGLY48
AGLY49
AILE50
APRO81
AALA82
BARG8

Functional Information from PROSITE/UniProt
site_idPS00141
Number of Residues12
DetailsASP_PROTEASE Eukaryotic and viral aspartyl proteases active site. ALLDTGADDTIF
ChainResidueDetails
AALA22-PHE33

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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