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1K2B

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 Residues38
DetailsBINDING SITE FOR RESIDUE 0Q4 A 401
ChainResidue
AARG8
AILE47
AGLY48
AGLY49
AILE50
APHE53
APRO81
AVAL82
AILE84
AHOH501
AHOH509
ALEU23
BARG8
BLEU23
BASP25
BGLY27
BALA28
BASP29
BASP30
BLYS45
BMET46
BILE47
AASP25
BGLY48
BGLY49
BILE50
BPRO81
BVAL82
BILE84
BHOH510
BHOH539
BHOH570
AGLY27
AALA28
AASP29
AASP30
ALYS45
AMET46

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
BASP25

site_idSWS_FT_FI2
Number of Residues2
DetailsSITE: Cleavage; by viral protease => ECO:0000250
ChainResidueDetails
APHE99
BPHE99

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 2024-07-17

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