Current Protein Identity:P0C6F2 New Search
Main Difference Dimensions in This Set
Different construct Different mutation/modification Different assembly state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics

Difference tags compare only the current result set; every original PDB and assembly record remains separate.

Related-Structure Differences

Each row represents one biological assembly in one PDB entry; multiple monomers of the same protein are listed separately.

PDB Entry Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Experimental Method Experimental Conditions Structure Quality
3LP3 p15 HIV RNaseH domain with inhibitor MK3 Deposited 2010-02-04 Assembly 1 Protein monomer Monomer;Protein × 1 PDB declaration: monomeric(1) Consistent with protein count
Chain A 1014–1149(136 aa) Fragment:residues 1014-1149
Not recorded MN MANGANESE (II) ION × 2 LP9 3-[4-(diethylamino)phenoxy]-6-(ethoxycarbonyl)-5,8-dihydroxy-7-oxo-7,8-dihydro-1,8-naphthyridin-1-ium × 1 X-RAY DIFFRACTION
X-ray crystallization conditions hanging drop;pH 6.8;298 K;0.1 M Sodium citrate pH 5.0, 15-20% PEG 8000, hanging drop, temperature 298K
Resolution 2.80 Å R-free 0.288
3LP3 p15 HIV RNaseH domain with inhibitor MK3 Deposited 2010-02-04 Assembly 2 Protein monomer Monomer;Protein × 1 PDB declaration: monomeric(1) Consistent with protein count
Chain B 1014–1149(136 aa) Fragment:residues 1014-1149
Not recorded MN MANGANESE (II) ION × 2 LP9 3-[4-(diethylamino)phenoxy]-6-(ethoxycarbonyl)-5,8-dihydroxy-7-oxo-7,8-dihydro-1,8-naphthyridin-1-ium × 1 X-RAY DIFFRACTION
X-ray crystallization conditions hanging drop;pH 6.8;298 K;0.1 M Sodium citrate pH 5.0, 15-20% PEG 8000, hanging drop, temperature 298K
Resolution 2.80 Å R-free 0.288
3LP3 p15 HIV RNaseH domain with inhibitor MK3 Deposited 2010-02-04 Assembly 3 Protein homooligomer Homooligomer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count
Chain A 1014–1149(136 aa) Fragment:residues 1014-1149
Chain B 1014–1149(136 aa) Fragment:residues 1014-1149
Not recorded MN MANGANESE (II) ION × 4 LP9 3-[4-(diethylamino)phenoxy]-6-(ethoxycarbonyl)-5,8-dihydroxy-7-oxo-7,8-dihydro-1,8-naphthyridin-1-ium × 2 X-RAY DIFFRACTION
X-ray crystallization conditions hanging drop;pH 6.8;298 K;0.1 M Sodium citrate pH 5.0, 15-20% PEG 8000, hanging drop, temperature 298K
Resolution 2.80 Å R-free 0.288
3TH9 Crystal Structure of HIV-1 Protease Mutant Q7K V32I L63I with a cyclic sulfonamide inhibitor Deposited 2011-08-18 Assembly 1 Protein homooligomer Homooligomer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count
Chain A 489–587(99 aa) Fragment:HIV protease
Chain B 489–587(99 aa) Fragment:HIV protease
Mutation:Q7K V32I L63I Mutation:Q7K V32I L63I 9Y9 tert-butyl {(2S,3R)-4-[(4S)-7-fluoro-4-methyl-1,1-dioxido-4,5-dihydro-1,2-benzothiazepin-2(3H)-yl]-3-hydroxy-1-phenylbutan-2-yl}carbamate × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP;pH 5.4;295 K;0.1 M sodium acetate buffer, 0.4M NaCl, pH 5.4, VAPOR DIFFUSION, HANGING DROP, temperature 295K
Resolution 1.34 Å R-free 0.190
3VFA Crystal Structure of HIV-1 Protease Mutant V82A with novel P1'-Ligands GRL-02031 Deposited 2012-01-09 Assembly 1 Protein homooligomer Homooligomer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count
Chain A 489–587(99 aa) Fragment:UNP residues 501-599
Chain B 489–587(99 aa) Fragment:UNP residues 501-599
Mutation:Q507K, L33I5, L563I, C567A, V582A, C595A Mutation:Q507K, L33I5, L563I, C567A, V582A, C595A 031 (3aS,5R,6aR)-hexahydro-2H-cyclopenta[b]furan-5-yl [(1S,2R)-1-benzyl-2-hydroxy-3-([(4-methoxyphenyl)sulfonyl]{[(2R)-5-oxopyrrolidin-2-yl]methyl}amino)propyl]carbamate × 1 NA SODIUM ION × 1 CL CHLORIDE ION × 8 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP;pH 4.8;298 K;0.6M NaCl, 0.1M Sodium Acetate buffer pH 4.8, VAPOR DIFFUSION, HANGING DROP, temperature 298K
Resolution 1.43 Å R-free 0.218
4I8W Crystal structure of wild type HIV-1 protease in complex with non-peptidic inhibitor, GRL007 Deposited 2012-12-04 Assembly 1 Protein homooligomer Homooligomer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count
Chain A 489–587(99 aa)
Chain B 489–587(99 aa)
Not recorded G07 4-{[(2R,3S)-3-({[(3R,3aS,6aR)-hexahydrofuro[2,3-b]furan-3-yloxy]carbonyl}amino)-2-hydroxy-4-phenylbutyl](2-methylpropyl)sulfamoyl}benzoic acid × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP;pH 9;298 K;1.6 M ammonium sulfate (precipitant) in 0.1 M BICINE buffer, pH 9.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K
Resolution 1.96 Å R-free 0.233
4I8Z Crystal structure of wild type HIV-1 protease in complex with non-peptidic inhibitor, GRL008 Deposited 2012-12-04 Assembly 1 Protein homooligomer Homooligomer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count
Chain A 489–587(99 aa)
Chain B 489–587(99 aa)
Not recorded G08 (3R,3aS,6aR)-hexahydrofuro[2,3-b]furan-3-yl [(2S,3R)-4-{[(4-carbamoylphenyl)sulfonyl](2-methylpropyl)amino}-3-hydroxy-1-phenylbutan-2-yl]carbamate × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP;pH 9;298 K;1.6 M ammonium sulfate (precipitant) in 0.1 M BICINE buffer, pH 9.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K
Resolution 1.75 Å R-free 0.220
4MC1 HIV protease in complex with SA526P Deposited 2013-08-21 Assembly 1 Protein homooligomer Homooligomer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count
Chain A 489–587(99 aa) Fragment:UNP residues 489-587
Chain B 489–587(99 aa) Fragment:UNP residues 489-587
Mutation:Q7K V32I L63I Mutation:Q7K V32I L63I CL CHLORIDE ION × 3 526 (3S)-tetrahydrofuran-3-yl {(2S,3R)-4-[(4S)-4-tert-butyl-7-fluoro-1,1-dioxido-4,5-dihydro-1,2-benzothiazepin-2(3H)-yl]-3-hydroxy-1-phenylbutan-2-yl}carbamate × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP;pH 5;295 K;0.7 M sodium chloride, 100 mM sodium citrate, pH 5.0, VAPOR DIFFUSION, HANGING DROP, temperature 295K
Resolution 1.39 Å R-free 0.188
4MC2 HIV protease in complex with SA525P Deposited 2013-08-21 Assembly 1 Protein homooligomer Homooligomer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count
Chain A 489–587(99 aa) Fragment:UNP residues 489-587
Chain B 489–587(99 aa) Fragment:UNP residues 489-587
Mutation:Q7K V32I L63I Mutation:Q7K V32I L63I 525 (3S)-tetrahydrofuran-3-yl {(2S,3R)-4-[(4R)-4-tert-butyl-7-fluoro-1,1-dioxido-4,5-dihydro-1,2-benzothiazepin-2(3H)-yl]-3-hydroxy-1-phenylbutan-2-yl}carbamate × 2 CL CHLORIDE ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP;pH 5;295 K;0.7 M sodium chloride, 100 mM sodium citrate, pH 5.0, VAPOR DIFFUSION, HANGING DROP, temperature 295K
Resolution 1.56 Å R-free 0.207
4MC6 HIV protease in complex with SA499 Deposited 2013-08-21 Assembly 1 Protein homooligomer Homooligomer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count
Chain A 489–587(99 aa) Fragment:UNP residues 489-587
Chain B 489–587(99 aa) Fragment:UNP residues 489-587
Mutation:Q7K V32I L63I Mutation:Q7K V32I L63I 23K 1-tert-butyl-3-{(2S,3R)-4-[(4R)-7-fluoro-1,1-dioxido-4-(propan-2-yl)-4,5-dihydro-1,2-benzothiazepin-2(3H)-yl]-3-hydroxy-1-phenylbutan-2-yl}urea × 1 EDO 1,2-ETHANEDIOL × 1 CL CHLORIDE ION × 3 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP;pH 5;295 K;0.7 M sodium chloride, 100 mM sodium citrate, pH 5.0, VAPOR DIFFUSION, HANGING DROP, temperature 295K
Resolution 1.31 Å R-free 0.198
4MC9 HIV protease in complex with AA74 Deposited 2013-08-21 Assembly 1 Protein homooligomer Homooligomer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count
Chain A 489–587(99 aa) Fragment:UNP residues 489-587
Chain B 489–587(99 aa) Fragment:UNP residues 489-587
Mutation:Q7K V32I L63I Mutation:Q7K V32I L63I 23L (3S)-tetrahydrofuran-3-yl {(2S,3R)-4-[(4R)-7-fluoro-1,1-dioxido-4-(propan-2-yl)-4,5-dihydro-1,2-benzothiazepin-2(3H)-yl]-3-hydroxy-1-phenylbutan-2-yl}carbamate × 2 EDO 1,2-ETHANEDIOL × 2 CL CHLORIDE ION × 3 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP;pH 5;295 K;0.7 M sodium chloride, 100 mM sodium citrate, pH 5.0, VAPOR DIFFUSION, HANGING DROP, temperature 295K
Resolution 1.19 Å R-free 0.195
4NYF HIV integrase in complex with inhibitor Deposited 2013-12-10 Assembly 1 Protein homooligomer Homooligomer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count
Chain A 1199–1357(159 aa) Fragment:Integrase catalytic domain residues 1199-1357
Chain B 1199–1357(159 aa) Fragment:Integrase catalytic domain residues 1199-1357
Mutation:C56S, W131D, F139D, F185K Mutation:C56S, W131D, F139D, F185K 4BI (2S)-tert-butoxy[4-(4-chlorophenyl)-2-methylquinolin-3-yl]ethanoic acid × 1 CD CADMIUM ION × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP;pH 5.6;297 K;1.2 -1.5 M Ammonium Sulfate, 100mM Na citrate pH 5.6, 50mM Cadmium chloride, VAPOR DIFFUSION, HANGING DROP, temperature 297K
Resolution 1.90 Å R-free 0.223
4QGI X-ray crystal structure of HIV-1 protease variant G48T/L89M in complex with Saquinavir Deposited 2014-05-22 Assembly 1 Protein homooligomer Homooligomer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count
Chain A 489–587(99 aa) Fragment:HIV-1 Protease Chain A, unp residues 489-587
Chain B 489–587(99 aa) Fragment:HIV-1 Protease Chain A, unp residues 489-587
Mutation:G48T, L89M Mutation:G48T, L89M ROC (2S)-N-[(2S,3R)-4-[(2S,3S,4aS,8aS)-3-(tert-butylcarbamoyl)-3,4,4a,5,6,7,8,8a-octahydro-1H-isoquinolin-2-yl]-3-hydroxy-1 -phenyl-butan-2-yl]-2-(quinolin-2-ylcarbonylamino)butanediamide × 1 GOL GLYCEROL × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP;pH 5.6;293 K;0.1 M Sodium citrate, 20% 2-propanol, 20% PEG 4000 , pH 5.6, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 1.90 Å R-free 0.246
5K14 HIV-1 Reverse Transcriptase in complex with a 2,6-difluorophenyl DAPY analog Deposited 2016-05-17 Assembly 1 Protein heterocomplex Heteromer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count
Chain B 588–1027(440 aa)
Not recorded IB1 4-{[4-(2,6-difluoro-4-methoxybenzene-1-carbonyl)pyrimidin-2-yl]amino}benzonitrile × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP;pH 6;293 K;1.0M K/Na tartrate 100mM MES pH 6.0
Resolution 2.40 Å R-free 0.261
6Y9V Structure of the native full-length HIV-1 capsid protein in complex with Cyclophilin A from helical assembly (-8,13) Deposited 2020-03-10 Assembly 1 Protein heterocomplex Heteromer;Protein × 13 PDB declaration: tridecameric(13) Consistent with protein count
Chain A 133–352(220 aa)
Chain B 133–352(220 aa)
Chain C 133–352(220 aa)
Chain D 133–352(220 aa)
Chain G 133–352(220 aa)
Chain H 133–352(220 aa)
Chain N 133–352(220 aa)
Chain Y 133–352(220 aa)
Chain d 133–352(220 aa)
Chain e 133–352(220 aa)
Chain j 133–352(220 aa)
Chain k 133–352(220 aa)
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 6.90 Å
6Y9W Structure of the native full-length HIV-1 capsid protein in complex with Cyclophilin A from helical assembly (-13,8) Deposited 2020-03-10 Assembly 1 Protein heterocomplex Heteromer;Protein × 13 PDB declaration: tridecameric(13) Consistent with protein count
Chain A 133–352(220 aa)
Chain B 133–352(220 aa)
Chain C 133–352(220 aa)
Chain D 133–352(220 aa)
Chain G 133–352(220 aa)
Chain H 133–352(220 aa)
Chain N 133–352(220 aa)
Chain Y 133–352(220 aa)
Chain d 133–352(220 aa)
Chain e 133–352(220 aa)
Chain j 133–352(220 aa)
Chain k 133–352(220 aa)
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 4.10 Å
6Y9X Structure of the native full-length HIV-1 capsid protein in complex with Cyclophilin A from helical assembly (-13,7) Deposited 2020-03-10 Assembly 1 Protein heterocomplex Heteromer;Protein × 13 PDB declaration: tridecameric(13) Consistent with protein count
Chain A 133–352(220 aa)
Chain B 133–352(220 aa)
Chain C 133–352(220 aa)
Chain D 133–352(220 aa)
Chain G 133–352(220 aa)
Chain H 133–352(220 aa)
Chain N 133–352(220 aa)
Chain Y 133–352(220 aa)
Chain d 133–352(220 aa)
Chain e 133–352(220 aa)
Chain j 133–352(220 aa)
Chain k 133–352(220 aa)
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 4.40 Å
6Y9Y Structure of the native full-length HIV-1 capsid protein in complex with Cyclophilin A from helical assembly (-7,13) Deposited 2020-03-10 Assembly 1 Protein heterocomplex Heteromer;Protein × 13 PDB declaration: tridecameric(13) Consistent with protein count
Chain A 133–352(220 aa)
Chain B 133–352(220 aa)
Chain C 133–352(220 aa)
Chain D 133–352(220 aa)
Chain G 133–352(220 aa)
Chain H 133–352(220 aa)
Chain N 133–352(220 aa)
Chain Y 133–352(220 aa)
Chain d 133–352(220 aa)
Chain e 133–352(220 aa)
Chain j 133–352(220 aa)
Chain k 133–352(220 aa)
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 6.10 Å
6Y9Z Structure of the native full-length HIV-1 capsid protein in complex with Cyclophilin A from helical assembly (-13,9) Deposited 2020-03-10 Assembly 1 Protein heterocomplex Heteromer;Protein × 13 PDB declaration: tridecameric(13) Consistent with protein count
Chain A 133–352(220 aa)
Chain B 133–352(220 aa)
Chain C 133–352(220 aa)
Chain D 133–352(220 aa)
Chain G 133–352(220 aa)
Chain H 133–352(220 aa)
Chain N 133–352(220 aa)
Chain Y 133–352(220 aa)
Chain d 133–352(220 aa)
Chain e 133–352(220 aa)
Chain j 133–352(220 aa)
Chain k 133–352(220 aa)
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 4.80 Å
9JA0 The capsid protein of HIV 1 Deposited 2024-08-23 Assembly 1 Protein homooligomer Homooligomer;Protein × 12 PDB declaration: dodecameric(12) Consistent with protein count
Chain A 133–353(221 aa)
Chain B 133–353(221 aa)
Chain C 133–353(221 aa)
Chain D 133–353(221 aa)
Chain E 133–353(221 aa)
Chain F 133–353(221 aa)
Chain G 133–353(221 aa)
Chain H 133–353(221 aa)
Chain I 133–353(221 aa)
Chain J 133–353(221 aa)
Chain K 133–353(221 aa)
Chain L 133–353(221 aa)
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.14 Å