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1IZI

Inhibitor of HIV protease with unusual binding mode potently inhibiting multi-resistant protease mutants

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 Residues2
DetailsBINDING SITE FOR RESIDUE CL A 100
ChainResidue
ATHR74
AASN88

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL B 100
ChainResidue
BGLY73
BTHR74
BASN88
BGLN92

site_idAC3
Number of Residues21
DetailsBINDING SITE FOR RESIDUE Q50 B 1001
ChainResidue
AASP30
AVAL32
AILE47
AGLY48
AGLY49
ATHR82
BASP25
BGLY27
BALA28
BASP29
BASP30
BILE47
BGLY48
BGLY49
BILE50
BPRO81
BHOH1002
BHOH1014
AARG8
AASP25
AGLY27

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

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

226707

PDB entries from 2024-10-30

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