Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

1HTG

X-RAY CRYSTALLOGRAPHIC STUDIES OF A SERIES OF PENICILLIN-DERIVED ASYMMETRIC INHIBITORS OF HIV-1 PROTEASE

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 Residues22
DetailsBINDING SITE FOR RESIDUE G37 A 300
ChainResidue
AASP25
AVAL82
AILE84
AHOH308
AHOH332
AG37600
BARG8
BLEU23
BASP25
BGLY27
BASP29
AGLY27
BASP30
BILE47
BILE50
AALA28
AASP29
AASP30
AVAL32
AILE47
AGLY48
AGLY49

site_idAC2
Number of Residues22
DetailsBINDING SITE FOR RESIDUE G37 A 600
ChainResidue
AARG8
ALEU23
AASP25
AGLY27
AASP30
AILE47
AGLY48
AILE50
AG37300
AHOH308
BASP25
BGLY27
BALA28
BASP29
BASP30
BVAL32
BILE47
BGLY48
BGLY49
BPHE53
BILE84
BHOH313

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
BILE64

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: Phosphotyrosine; by host => ECO:0000250
ChainResidueDetails
AILE64
BILE64

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

222926

PDB entries from 2024-07-24

PDB statisticsPDBj update infoContact PDBjnumon