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3NDU

HIV-1 Protease Saquinavir:Ritonavir 1:5 complex structure

Functional Information from GO Data
ChainGOidnamespacecontents
A0004190molecular_functionaspartic-type endopeptidase activity
A0006508biological_processproteolysis
B0004190molecular_functionaspartic-type endopeptidase activity
B0006508biological_processproteolysis
C0004190molecular_functionaspartic-type endopeptidase activity
C0006508biological_processproteolysis
D0004190molecular_functionaspartic-type endopeptidase activity
D0006508biological_processproteolysis
Functional Information from PDB Data
site_idAC1
Number of Residues32
DetailsBINDING SITE FOR RESIDUE ROC A 101
ChainResidue
AARG9
AILE51
ATHR81
APRO82
AILE85
AHOH119
AHOH570
BARG9
BASP26
BGLY28
BALA29
AASP26
BASP30
BASP31
BGLY49
BGLY50
BILE51
BTHR81
BPRO82
BVAL83
BILE85
BHOH103
AGLY28
BHOH107
BHOH153
CTRP6
AALA29
AASP30
AASP31
AILE48
AGLY49
AGLY50

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE DMS A 102
ChainResidue
ALYS15
AILE16
AGLY18
AILE64
BGLY18
BDMS101

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ACT A 1007
ChainResidue
ATHR13
AGLU66
AALA68
AGLY69
ANA1015

site_idAC4
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CL A 1010
ChainResidue
BLYS71

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE GOL A 1012
ChainResidue
AGLN3
AILE4
ATHR5

site_idAC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE NA A 1015
ChainResidue
AGLY69
AHOH112
AACT1007

site_idAC7
Number of Residues2
DetailsBINDING SITE FOR RESIDUE ACT A 1017
ChainResidue
ATRP7
BARG88

site_idAC8
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL A 1021
ChainResidue
ALYS44
ALYS46
AGLN59

site_idAC9
Number of Residues8
DetailsBINDING SITE FOR RESIDUE DMS B 101
ChainResidue
ALYS15
AGLY18
ADMS102
BLYS15
BILE16
BGLY17
BGLY18
BILE64

site_idBC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL B 1001
ChainResidue
BLYS46
BMET47
BHOH104
BHOH212
DHOH107

site_idBC2
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CL B 1003
ChainResidue
BSER38

site_idBC3
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CL B 1005
ChainResidue
ASER38

site_idBC4
Number of Residues1
DetailsBINDING SITE FOR RESIDUE NA B 1014
ChainResidue
BASP61

site_idBC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ACT B 1016
ChainResidue
BLEU11
BVAL12
BTHR13
BHOH576
CTRP42

site_idBC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE NA B 1020
ChainResidue
AHIS70
AILE94
BPHE100

site_idBC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE DMS C 100
ChainResidue
CLYS14
CGLY16
CGLY17
CILE63
DGLY17
DDMS101

site_idBC8
Number of Residues5
DetailsBINDING SITE FOR RESIDUE DMS C 101
ChainResidue
CMET36
CSER37
DPRO39
DGLY40
DHOH203

site_idBC9
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL C 1006
ChainResidue
ALYS71
BLYS15
CLYS55

site_idCC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ACT C 1008
ChainResidue
CTHR4
CTRP6
CHOH301
DTHR91
DGLY94

site_idCC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL C 1013
ChainResidue
CHOH578
DGLY51
DHOH541
CPRO79

site_idCC3
Number of Residues31
DetailsBINDING SITE FOR RESIDUE ROC D 100
ChainResidue
CARG8
CASP25
CGLY27
CALA28
CASP29
CASP30
CVAL32
CILE47
CGLY48
CGLY49
CILE50
CTHR80
CPRO81
CILE84
CHOH129
CHOH573
DASP25
DGLY27
DALA28
DASP29
DASP30
DVAL32
DILE47
DGLY48
DGLY49
DILE50
DTHR80
DPRO81
DILE84
DHOH115
DHOH150

site_idCC4
Number of Residues8
DetailsBINDING SITE FOR RESIDUE DMS D 101
ChainResidue
CGLY17
CDMS100
DLYS14
DILE15
DGLY16
DGLY17
DILE63
DGLU65

Functional Information from PROSITE/UniProt
site_idPS00141
Number of Residues12
DetailsASP_PROTEASE Eukaryotic and viral aspartyl proteases active site. ALLDTGADDTVI
ChainResidueDetails
AALA23-ILE34

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: For protease activity; shared with dimeric partner => ECO:0000255|PROSITE-ProRule:PRU10094
ChainResidueDetails
AASP26
BASP26
CASP25
DASP25

site_idSWS_FT_FI2
Number of Residues4
DetailsSITE: Cleavage; by viral protease => ECO:0000250
ChainResidueDetails
APHE100
BPHE100
CPHE99
DPHE99

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PDB entries from 2024-09-11

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