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2P3C

Crystal Structure of the subtype F 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 Residues42
DetailsBINDING SITE FOR RESIDUE 3TL A 201
ChainResidue
AARG8
AILE47
AGLY48
AGLY48
AGLY49
AILE50
APHE53
APRO81
APRO81
AVAL82
AILE84
AASP25
AHOH303
AHOH334
AHOH344
BARG8
BASP25
BGLY27
BALA28
BASP29
BASP30
BVAL32
AGLY27
BLYS45
BMET46
BILE47
BGLY48
BGLY48
BGLY49
BILE50
BPHE53
BPHE53
BPRO81
AALA28
BPRO81
BVAL82
BILE84
AASP29
AASP30
AVAL32
ALYS45
AMET46

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ACY B 301
ChainResidue
BLYS14
BGLY16
BGLY17
BHOH327

site_idAC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE ACY A 302
ChainResidue
ATHR12
ALYS14
AGLU65
ACME67
AGLY68
BTHR12
BCME67
BACY303

site_idAC4
Number of Residues8
DetailsBINDING SITE FOR RESIDUE ACY B 303
ChainResidue
ATHR12
ACME67
AACY302
BTHR12
BLYS14
BGLU65
BCME67
BGLY68

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

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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