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1K1T

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 Residues41
DetailsBINDING SITE FOR RESIDUE 0Q4 B 201
ChainResidue
ATRP6
AILE47
AGLY48
AGLY49
AILE50
APHE53
APRO81
ASER82
AILE84
AHOH569
BARG108
AARG8
BLEU123
BASP125
BGLY127
BALA128
BASP129
BASP130
BVAL132
BMET146
BILE147
BGLY148
AASP25
BGLY149
BILE150
BPRO181
BSER182
BILE184
BHOH419
BHOH441
BHOH451
BHOH497
BHOH538
AGLY27
BHOH554
BHOH570
AALA28
AASP29
AASP30
AVAL32
AMET46

site_idAC2
Number of Residues9
DetailsBINDING SITE FOR RESIDUE SO4 B 401
ChainResidue
ALYS14
AILE15
AGLY16
AGLY17
AHOH423
AHOH525
BLYS114
BGLY117
BHOH458

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
ATHR26
BTHR126

site_idSWS_FT_FI2
Number of Residues2
DetailsSITE: Cleavage; by viral protease => ECO:0000250
ChainResidueDetails
APRO1
BPRO101

218853

PDB entries from 2024-04-24

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