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2P3B

Crystal Structure of the subtype B wild type HIV protease complexed with TL-3 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 Residues34
DetailsBINDING SITE FOR RESIDUE 3TL A 101
ChainResidue
AARG8
AGLY49
AILE50
APHE53
APRO81
APRO81
AVAL82
AILE84
AHOH102
AHOH107
BARG8
AASP25
BASP25
BGLY27
BALA28
BASP29
BMET46
BILE47
BGLY48
BGLY49
BILE50
BPHE53
AGLY27
BPRO81
BPRO81
BVAL82
BILE84
BHOH105
AALA28
AASP29
AMET46
AILE47
AGLY48
AGLY48

Functional Information from PROSITE/UniProt
site_idPS00141
Number of Residues12
DetailsASP_PROTEASE Eukaryotic and viral aspartyl proteases active site. ALLDTGADDTVL
ChainResidueDetails
AALA22-LEU33
BALA22-LEU33

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: For protease activity; shared with dimeric partner => ECO:0000255|PROSITE-ProRule:PRU10094
ChainResidueDetails
BASP25

site_idSWS_FT_FI2
Number of Residues1
DetailsSITE: Cleavage; by viral protease => ECO:0000250
ChainResidueDetails
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 2024-07-31

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