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1ZPK

Crystal structure of the complex of mutant HIV-1 protease (A71V, V82T, I84V) with a hydroxyethylamine peptidomimetic inhibitor BOC-PHE-PSI[R-CH(OH)CH2NH]-PHE-GLU-PHE-NH2

Functional Information from GO Data
ChainGOidnamespacecontents
A0004190molecular_functionaspartic-type endopeptidase activity
A0006508biological_processproteolysis
A0008233molecular_functionpeptidase activity
A0016787molecular_functionhydrolase activity
B0004190molecular_functionaspartic-type endopeptidase activity
B0006508biological_processproteolysis
B0008233molecular_functionpeptidase activity
B0016787molecular_functionhydrolase activity
Functional Information from PDB Data
site_idAC1
Number of Residues33
DetailsBINDING SITE FOR RESIDUE 0ZS A 201
ChainResidue
AARG8
AGLY49
AILE50
APHE53
APRO81
ATHR82
AHOH301
AHOH392
AHOH415
AHOH416
BLEU123
ALEU23
BASP125
BGLY127
BALA128
BASP129
BASP130
BILE147
BGLY148
BGLY149
BILE150
BPRO181
AASP25
BTHR182
BHOH302
BHOH327
BHOH410
AGLY27
AALA28
AASP29
AASP30
AILE47
AGLY48

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL B 501
ChainResidue
BGLY173
BTHR174
BASN188

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE NA B 502
ChainResidue
BASP130
BHOH308
BHOH362

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
DetailsSITE: Cleavage; by viral protease => ECO:0000250
ChainResidueDetails
AILE64
BILE164

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: Phosphotyrosine; by host => ECO:0000250
ChainResidueDetails
AILE64
BILE164

218853

PDB entries from 2024-04-24

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