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

3NDX

HIV-1 Protease Saquinavir:Ritonavir 1:50 complex structure

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 Residues26
DetailsBINDING SITE FOR RESIDUE RIT A 100
ChainResidue
AARG8
APRO81
AHOH110
AHOH164
AHOH216
AGOL1041
BASP25
BGLY27
BALA28
BASP29
BILE47
AASP25
BGLY48
BGLY49
BILE50
BVAL82
BILE84
BHOH125
BHOH221
AGLY27
AALA28
AASP29
AASP30
AGLY48
AGLY49
AILE50

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE DMS A 991
ChainResidue
AGLN92
AHOH170
AHOH210
BGLY49
BGLY52
BPHE53
BHOH171

site_idAC3
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL A 1041
ChainResidue
ATRP6
AGLY48
ARIT100
AHOH122
AHOH145
AHOH171
AHOH277
BPRO81
BHOH123

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL A 308
ChainResidue
ALYS7
AARG8
AHOH305
BHOH307

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 B 100
ChainResidue
BPRO1
BARG57
BHIS69
BHOH138
BHOH139
BHOH284

site_idAC6
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL B 101
ChainResidue
BVAL11
BTHR12
BTRP42
BALA67
BHOH137
BHOH176
BHOH181
BHOH342

site_idAC7
Number of Residues7
DetailsBINDING SITE FOR RESIDUE DMS B 992
ChainResidue
AGLY17
BLYS14
BILE15
BGLY16
BGLY17
BILE63
BGLU65

site_idAC8
Number of Residues9
DetailsBINDING SITE FOR RESIDUE DMS B 993
ChainResidue
APRO39
AGLY40
AHOH142
AHOH223
AHOH323
BMET36
BSER37
BHOH111
BHOH172

site_idAC9
Number of Residues7
DetailsBINDING SITE FOR RESIDUE DMS B 994
ChainResidue
ALYS14
AILE15
AGLY16
AGLY17
AILE63
AHOH271
BLYS14

site_idBC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 B 1040
ChainResidue
APRO1
ALYS55
BHIS69
BLYS70
BHOH170
BHOH203
BHOH237

Functional Information from PROSITE/UniProt
site_idPS00141
Number of Residues12
DetailsASP_PROTEASE Eukaryotic and viral aspartyl proteases active site. ALLDTGADDTVI
ChainResidueDetails
AALA22-ILE33

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

224931

PDB entries from 2024-09-11

PDB statisticsPDBj update infoContact PDBjnumon