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1IZH

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
A0008233molecular_functionpeptidase activity
A0016787molecular_functionhydrolase activity
A0055036cellular_componentvirion membrane
A0072494cellular_componenthost multivesicular body
B0004190molecular_functionaspartic-type endopeptidase activity
B0006508biological_processproteolysis
B0008233molecular_functionpeptidase activity
B0016787molecular_functionhydrolase activity
B0055036cellular_componentvirion membrane
B0072494cellular_componenthost multivesicular body
Functional Information from PDB Data
site_idAC1
Number of Residues34
DetailsBINDING SITE FOR RESIDUE Q50 B 1001
ChainResidue
AARG8
AILE50
APHE53
APRO81
AVAL82
AILE84
AHOH192
BARG8
BLEU23
BASP25
BGLY27
AASP25
BALA28
BASP29
BASP30
BILE47
BGLY48
BGLY49
BILE50
BPHE53
BVAL82
BILE84
AGLY27
BHOH1017
BHOH1018
BHOH1032
BHOH1064
BHOH1068
AALA28
AASP29
AASP30
AILE47
AGLY48
AGLY49

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

251174

PDB entries from 2026-03-25

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