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1K1U

Combining Mutations in HIV-1 Protease to Understand Mechanisms of Resistance

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 Residues40
DetailsBINDING SITE FOR RESIDUE 0Q4 B 301
ChainResidue
AARG8
AMET46
AILE47
AGLY48
AGLY49
AILE50
AGLN58
AVAL82
AILE84
BARG108
BLEU123
ALEU23
BASP125
BGLY127
BALA128
BASP129
BASP130
BVAL132
BILE145
BMET146
BILE147
BGLY148
AASP25
BGLY149
BILE150
BGLN161
BPRO181
BVAL182
BILE184
BHOH540
BHOH572
BHOH580
BHOH613
AGLY27
BHOH633
AALA28
AASP29
AASP30
AVAL32
AILE45

Functional Information from PROSITE/UniProt
site_idPS00141
Number of Residues12
DetailsASP_PROTEASE Eukaryotic and viral aspartyl proteases active site. ALLDTGADDTVI
ChainResidueDetails
AALA22-ILE33

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: For protease activity; shared with dimeric partner => ECO:0000255|PROSITE-ProRule:PRU10094
ChainResidueDetails
AASP25
BASP125

site_idSWS_FT_FI2
Number of Residues2
DetailsSITE: Cleavage; by viral protease => ECO:0000250
ChainResidueDetails
APHE99
BPHE199

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1a30
ChainResidueDetails
AASP25
ATHR26
BTHR126
BASP125

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1a30
ChainResidueDetails
AASP25
BASP125

223790

PDB entries from 2024-08-14

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