3ow4

Discovery of dihydrothieno- and dihydrofuropyrimidines as potent pan Akt inhibitors

Method: X-RAY DIFFRACTION D_max: 95.9 Å Quality: EXCELLENT

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1. Protein Identity and Related Structures Protein Identity & Related Structures

RAC-alpha serine/threonine-protein kinase

Homo sapiens

State in the Current Structure

Assembly	Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Associated Components	Method and Experimental Conditions	Structure Quality
1	Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain A； UniProt 144–480	Mutation：S473D Non-standard monomer：Yes (specific site not provided by mmCIF)	GSK 3 beta peptide × 1 SMY (2R)-3-(1H-indol-3-yl)-1-{4-[(5S)-5-methyl-5,7-dihydrothieno[3,4-d]pyrimidin-4-yl]piperazin-1-yl}-1-oxopropan-2-amine × 1	X-RAY DIFFRACTION X-ray crystallization conditions：Under oil；pH 7.5；293 K；8.3 mg/ml AKT1 protein, preincubated with 0.6 mM GSK3B peptide, 5 mM Mn-AMP-PNP. The precipitant was 20% PEG 4K, 15% isopropanol, 100 mM Hepes, pH 7.5, Under oil, temperature 293K	Resolution 2.60 Å R-free 0.268
2	Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain B； UniProt 144–480	Mutation：S473D Non-standard monomer：Yes (specific site not provided by mmCIF)	GSK 3 beta peptide × 1 SMY (2R)-3-(1H-indol-3-yl)-1-{4-[(5S)-5-methyl-5,7-dihydrothieno[3,4-d]pyrimidin-4-yl]piperazin-1-yl}-1-oxopropan-2-amine × 1	X-RAY DIFFRACTION X-ray crystallization conditions：Under oil；pH 7.5；293 K；8.3 mg/ml AKT1 protein, preincubated with 0.6 mM GSK3B peptide, 5 mM Mn-AMP-PNP. The precipitant was 20% PEG 4K, 15% isopropanol, 100 mM Hepes, pH 7.5, Under oil, temperature 293K	Resolution 2.60 Å R-free 0.268

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

Other PDB	Difference from Current Entry 3OW4	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1H10 HIGH RESOLUTION STRUCTURE OF THE PLECKSTRIN HOMOLOGY DOMAIN OF PROTEIN KINASE B/AKT BOUND TO INS(1,3,4,5)-TETRAKISPHOPHATE Deposited 2002-07-01	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–123（123 aa） Fragment：PLECKSTRIN HOMOLOGY DOMAIN, RESIDUES 1-123	Non-standard monomer：Yes (specific site not provided by mmCIF)	4IP INOSITOL-(1,3,4,5)-TETRAKISPHOSPHATE × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 4.2；0.25M AMMONIUM ACETATE, 30% PEG 4000,0.1M SODIUM ACETATE (PH 4.6)	Resolution 1.40 Å R-free 0.175
1UNP Crystal structure of the pleckstrin homology domain of PKB alpha Deposited 2003-09-12	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–121（121 aa） Fragment：PLECKSTRIN HOMOLOGY DOMAIN, RESIDUES 1-121	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions pH 8.5；30 % PEG 4000, 0.25 M SODIUM ACETATE, 0.1 M TRIS PH 8.5 3.3 % POLYPROPYLENE GLYCOL 400	Resolution 1.65 Å R-free 0.236
1UNQ High resolution crystal structure of the Pleckstrin Homology Domain Of Protein Kinase B/Akt Bound To Ins(1,3,4,5)-Tetrakisphophate Deposited 2003-09-12	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–123（123 aa） Fragment：PLECKSTRIN HOMOLOGY DOMAIN RESIDUES 1-123	Non-standard monomer：Yes (specific site not provided by mmCIF)	4IP INOSITOL-(1,3,4,5)-TETRAKISPHOSPHATE × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 4.6；0.25 M AMMONIUM ACETATE, 30 % PEG 4000, 0.1 M SODIUM ACETATE (4.6), pH 4.60	Resolution 0.98 Å R-free 0.179
1UNR Crystal structure of the PH domain of PKB alpha in complex with a sulfate molecule Deposited 2003-09-15	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–123（123 aa） Fragment：PLECKSTRIN HOMOLOGY DOMAIN, RESIDUES 1-123	Non-standard monomer：Yes (specific site not provided by mmCIF)	SO4 SULFATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 8.5；0.1 M TRIS (8.5) 0.2 M AMMONIUM SULFATE, pH 8.50	Resolution 1.25 Å R-free 0.226
2UVM Structure of PKBalpha PH domain in complex with a novel inositol headgroup surrogate, benzene 1,2,3,4-tetrakisphosphate Deposited 2007-03-12	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–123（123 aa） Fragment：PLECKSTRIN HOMOLOGY (PH) DOMAIN, RESIDUES 1-123	Not recorded	GVF BENZENE-1,2,3,4-TETRAYL TETRAKIS[DIHYDROGEN (PHOSPHATE)] × 1 NA SODIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 5；25-30% POLYETHYLENE GLYCOL 3000, 0.1 M SODIUM ACETATE TRIHYDRATE [PH 4.4-5.0], 0.2 M AMMONIUM ACETATE	Resolution 1.94 Å R-free 0.269
2UZR A transforming mutation in the pleckstrin homology domain of AKT1 in cancer (AKT1-PH_E17K) Deposited 2007-05-01	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–123（123 aa） Fragment：RESIDUES 1-123	Mutation：YES	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；0.1 M HEPES PH 7.5 AND 1.4 M SODIUM CITRATE, OR 0.1 M SODIUM ACETATE PH 4.6, 0.2 M AMMONIUM ACETATE AND 15%-30% PEG 3350,	Resolution 1.94 Å R-free 0.257
2UZS A transforming mutation in the pleckstrin homology domain of AKT1 in cancer (AKT1-PH_E17K) Deposited 2007-05-01	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–123（123 aa） Fragment：RESIDUES 1-123	Mutation：E17K Non-standard monomer：Yes (specific site not provided by mmCIF)	4IP INOSITOL-(1,3,4,5)-TETRAKISPHOSPHATE × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；GROWN FROM HANGING DROPS IN 0.1 M HEPES PH 7.5 AND 1.4 M SODIUM CITRATE, OR 0.1 M ACETATE PH 4.6, 0.2 M AMMONIUM ACETATE AND 15%-30% PEG 3350,	Resolution 2.46 Å R-free 0.286
3CQU Crystal Structure of Akt-1 complexed with substrate peptide and inhibitor Deposited 2008-04-03	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 144–480（337 aa） Fragment：Kinase and AGC-kinase C-terminal domains	Mutation：S473D Non-standard monomer：Yes (specific site not provided by mmCIF)	CQU N-[2-(5-methyl-4H-1,2,4-triazol-3-yl)phenyl]-7H-pyrrolo[2,3-d]pyrimidin-4-amine × 1	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.20 Å R-free 0.283
3CQW Crystal Structure of Akt-1 complexed with substrate peptide and inhibitor Deposited 2008-04-03	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 144–480（337 aa） Fragment：Kinase and AGC-kinase C-terminal domains	Mutation：S473D Non-standard monomer：Yes (specific site not provided by mmCIF)	MN MANGANESE (II) ION × 1 CQW 5-(5-chloro-7H-pyrrolo[2,3-d]pyrimidin-4-yl)-4,5,6,7-tetrahydro-1H-imidazo[4,5-c]pyridine × 1	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.00 Å R-free 0.257
3O96 Crystal Structure of Human AKT1 with an Allosteric Inhibitor Deposited 2010-08-03	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 2–443（442 aa） Fragment：unp residues 2-443	Not recorded	IQO 1-(1-(4-(7-phenyl-1H-imidazo[4,5-g]quinoxalin-6-yl)benzyl)piperidin-4-yl)-1H-benzo[d]imidazol-2(3H)-one × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.2；293 K；50 mM acetate-citrate buffer, 21% PEG MME 2000, pH 5.2, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 2.70 Å R-free 0.308
3QKK Spirochromane Akt Inhibitors Deposited 2011-02-01	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 144–480（337 aa） Fragment：kinase domain	Mutation：S473D Non-standard monomer：Yes (specific site not provided by mmCIF)	SMH N-(2-ethoxyethyl)-N-{(2S)-2-hydroxy-3-[(2R)-6-hydroxy-4-oxo-3,4-dihydro-1'H-spiro[chromene-2,3'-piperidin]-1'-yl]propyl}-2,6-dimethylbenzenesulfonamide × 1	X-RAY DIFFRACTION X-ray crystallization conditions Under oil；pH 7.8；293 K；8.1mg/ml protein, 0.6mM GSK-3 beta peptide, 5mM Mg-AMPPNP, 10mM DTT, 20% PEG 4K, 10% Isopropanol, 0.1M Hepes, pH 7.8, Under oil, temperature 293K	Resolution 2.30 Å R-free 0.250
3QKL Spirochromane Akt Inhibitors Deposited 2011-02-01	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 144–480（337 aa） Fragment：kinase domain	Mutation：S473D Non-standard monomer：Yes (specific site not provided by mmCIF)	SMR N-{(2S)-3-[(3S)-8',9'-dihydro-1H,3'H-spiro[piperidine-3,7'-pyrano[3,2-e]indazol]-1-yl]-2-hydroxypropyl}-N-(2-ethoxyethyl)-2,6-dimethylbenzenesulfonamide × 1	X-RAY DIFFRACTION X-ray crystallization conditions Under oil；pH 7.8；293 K；9.7mg/ml protein, 0.6mM GSK-3 beta peptide, 1mM Mg-AMPPNP, 10mM DTT, 22% PEG 4K, 10% Isopropanol, 0.1M Hepes, pH 7.8, Under oil, temperature 293K	Resolution 1.90 Å R-free 0.243
3QKM Spirocyclic sulfonamides as AKT inhibitors Deposited 2011-02-01	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 144–480（337 aa） Fragment：kinase domain	Mutation：S473D Non-standard monomer：Yes (specific site not provided by mmCIF)	SM9 N-(2-ethoxyethyl)-N-{(2S)-2-hydroxy-3-[(5R)-2-(quinazolin-4-yl)-2,7-diazaspiro[4.5]dec-7-yl]propyl}-2,6-dimethylbenzenesulfonamide × 1	X-RAY DIFFRACTION X-ray crystallization conditions Under oil；pH 7.8；293 K；9.7mg/ml protein, 0.6mM GSK-3 beta peptide, 1mM Mg-AMPPNP, 10mM DTT, 22% PEG 4K, 10% Isopropanol, 0.1M Hepes, pH 7.8, Under oil, temperature 293K	Resolution 2.20 Å R-free 0.252
4EJN Crystal structure of autoinhibited form of AKT1 in complex with N-(4-(5-(3-acetamidophenyl)-2-(2-aminopyridin-3-yl)-3H-imidazo[4,5-b]pyridin-3-yl)benzyl)-3-fluorobenzamide Deposited 2012-04-06	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 2–446（445 aa）	Mutation：E114A, E115A, E116A	0R4 N-(4-{5-[3-(acetylamino)phenyl]-2-(2-aminopyridin-3-yl)-3H-imidazo[4,5-b]pyridin-3-yl}benzyl)-3-fluorobenzamide × 1 SBT 2-BUTANOL × 1 EDO 1,2-ETHANEDIOL × 1	X-RAY DIFFRACTION X-ray crystallization conditions EVAPORATION；pH 7.5；277 K；16% butanol, 10mM ammonium sulfate, 0.1% 2-mercaptoethanol, 15% ethylene glycol, 50mM Tris , pH 7.5, EVAPORATION, temperature 277K	Resolution 2.19 Å R-free 0.276
4EKK Akt1 with AMP-PNP Deposited 2012-04-09	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 144–480（337 aa） Fragment：UNP residues 144-480	Mutation：S473D Non-standard monomer：Yes (specific site not provided by mmCIF)	ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 1 MN MANGANESE (II) ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions pH 7.5；293 K；20% PEG4K, 100mM Tris-pH7.5, Under Oil, temperature 293K	Resolution 2.80 Å R-free 0.280
4EKK Akt1 with AMP-PNP Deposited 2012-04-09	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 144–480（337 aa） Fragment：UNP residues 144-480	Mutation：S473D Non-standard monomer：Yes (specific site not provided by mmCIF)	ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 1 MN MANGANESE (II) ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions pH 7.5；293 K；20% PEG4K, 100mM Tris-pH7.5, Under Oil, temperature 293K	Resolution 2.80 Å R-free 0.280
4EKL Akt1 with GDC0068 Deposited 2012-04-09	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 144–480（337 aa） Fragment：UNP residues 144-480	Mutation：S473D Non-standard monomer：Yes (specific site not provided by mmCIF)	0RF (2S)-2-(4-chlorophenyl)-1-{4-[(5R,7R)-7-hydroxy-5-methyl-6,7-dihydro-5H-cyclopenta[d]pyrimidin-4-yl]piperazin-1-yl}-3-(propan-2-ylamino)propan-1-one × 1	X-RAY DIFFRACTION X-ray crystallization conditions Under Oil；pH 7.5；293 K；20% PEG4K 100mM Tris-pH7.5, Under Oil, temperature 293K	Resolution 2.00 Å R-free 0.235
4GV1 PKB alpha in complex with AZD5363 Deposited 2012-08-30	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 144–480（337 aa） Fragment：kinase domain (UNP residues 144-480)	Non-standard monomer：Yes (specific site not provided by mmCIF)	0XZ 4-amino-N-[(1S)-1-(4-chlorophenyl)-3-hydroxypropyl]-1-(7H-pyrrolo[2,3-d]pyrimidin-4-yl)piperidine-4-carboxamide × 1 GOL GLYCEROL × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.9；277 K；alcohol, pH 6.9, VAPOR DIFFUSION, SITTING DROP, temperature 277K	Resolution 1.49 Å R-free 0.210
5KCV Crystal structure of allosteric inhibitor, ARQ 092, in complex with autoinhibited form of AKT1 Deposited 2016-06-07	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 2–446（445 aa）	Mutation：E114A, E115A, E116A	6S1 3-[3-[4-(1-azanylcyclobutyl)phenyl]-5-phenyl-imidazo[4,5-b]pyridin-2-yl]pyridin-2-amine × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；277 K；16% butanol, 10mM ammonium sulfate, 0.1% 2-mercaptoethanol, 15% ethylene glycol, 50mM Tris, pH 7.5	Resolution 2.70 Å R-free 0.269
6BUU Crystal structure of AKT1 (aa 144-480) with a bisubstrate Deposited 2017-12-11	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 144–480（337 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF)	SO4 SULFATE ION × 1 MN MANGANESE (II) ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 7.5；277 K；20% PEG 3000, 0.1M Hepes HCL, 0.2M Ammonium sulfate	Resolution 2.40 Å R-free 0.230
6BUU Crystal structure of AKT1 (aa 144-480) with a bisubstrate Deposited 2017-12-11	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 144–480（337 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF)	MN MANGANESE (II) ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 7.5；277 K；20% PEG 3000, 0.1M Hepes HCL, 0.2M Ammonium sulfate	Resolution 2.40 Å R-free 0.230
6CCY Crystal structure of Akt1 in complex with a selective inhibitor Deposited 2018-02-07	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric	Chain A 144–466（323 aa）	Mutation：N199S, S396P, E397S, T433V Non-standard monomer：Yes (specific site not provided by mmCIF)	EX4 (5R)-4-(4-{4-[4-fluoro-3-(trifluoromethyl)phenyl]-1-[2-(pyrrolidin-1-yl)ethyl]-1H-imidazol-2-yl}piperidin-1-yl)-5-methyl-5,8-dihydropyrido[2,3-d]pyrimidin-7(6H)-one × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；277 K；16% PEG 3350 and 200mM Ammonium Formate	Resolution 2.18 Å R-free 0.276
6HHF Crystal Structure of AKT1 in Complex with Covalent-Allosteric AKT Inhibitor Borussertib Deposited 2018-08-28	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 2–446（445 aa）	Not recorded	G4K Borussertib × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.2；293 K；1.25 mM Na-acetate, 3.75 mM Na-citrate, 15% v/v PEG 2000 MME, pH 5.2, 3 mg/mL Akt1 (in 25 mM TRIS, 100 mM NaCl, 10 % Glycerol, 5 mM DTT, pH 7.5), 1 uL reservoir + 1 uL protein solution	Resolution 2.90 Å R-free 0.274
6HHG Crystal Structure of AKT1 in Complex with Covalent-Allosteric AKT Inhibitor 27 Deposited 2018-08-28	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 2–446（445 aa）	Not recorded	G4T ~{N}-[2-chloranyl-5-[[1-[[4-(5-oxidanylidene-3-phenyl-6~{H}-1,6-naphthyridin-2-yl)phenyl]methyl]piperidin-4-yl]carbamoylamino]phenyl]propanamide × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；293 K；1.25 mM Na-acetate, 3.75 mM Na-citrate, 15% v/v PEG 2000 MME, pH 7.5, 3 mg/mL Akt1 (in 25 mM TRIS, 100 mM NaCl, 10 % Glycerol, 5 mM DTT, pH 7.5), 1 uL reservoir + 1 uL protein solution	Resolution 2.30 Å R-free 0.246
6HHH Crystal Structure of AKT1 in Complex with Covalent-Allosteric AKT Inhibitor 31 Deposited 2018-08-28	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 2–446（445 aa）	Not recorded	G4Q ~{N}-[4-[4-[[4-(5-oxidanylidene-3-phenyl-6~{H}-1,6-naphthyridin-2-yl)phenyl]methyl]piperazin-1-yl]phenyl]propanamide × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；293 K；1.25 mM Na-acetate, 3.75 mM Na-citrate, 15% v/v PEG 2000 MME, pH 7.5, 3 mg/mL Akt1, (in 25 mM TRIS, 100 mM NaCl, 10 % Glycerol, 5 mM DTT, pH 7.5), 1ul reservoir + 1ul protein solution	Resolution 2.70 Å R-free 0.266
6HHI Crystal Structure of AKT1 in Complex with Covalent-Allosteric AKT Inhibitor 30b Deposited 2018-08-28	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 2–446（445 aa）	Not recorded	G4N ~{N}-[1-[[4-(5-oxidanylidene-3-phenyl-6~{H}-1,6-naphthyridin-2-yl)phenyl]methyl]piperidin-4-yl]-3-(propanoylamino)benzamide × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；293 K；1.25 mM Na-acetate, 3.75 mM Na-citrate, 21% v/v PEG 2000 MME, pH 6.5, 3 mg/mL Akt1 (in 25 mM TRIS, 100 mM NaCl, 10 % Glycerol, 5 mM DTT, pH 7.5), 1ul reservoir + 1ul protein solution	Resolution 2.70 Å R-free 0.258
6HHJ Crystal Structure of AKT1 in Complex with Covalent-Allosteric AKT Inhibitor 24b Deposited 2018-08-28	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 2–446（445 aa）	Not recorded	G4H ~{N}-[1-methyl-2-oxidanylidene-3-[1-[[4-(5-oxidanylidene-3-phenyl-6~{H}-1,6-naphthyridin-2-yl)phenyl]methyl]piperidin-4-yl]benzimidazol-5-yl]propanamide × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；293 K；1.25 mM Na-acetate, 3.75 mM Na-citrate, 15 % v/v PEG 2000 MME, pH 7.5, 3 mg/mL Akt1 (in 25 mM TRIS, 100 mM NaCl, 10 % Glycerol, 5 mM DTT, pH 7.5), 1ul reservoir + 1ul protein solution	Resolution 2.30 Å R-free 0.243
6NPZ Crystal structure of Akt1 (aa 123-480) kinase with a bisubstrate Deposited 2019-01-18	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 123–480（358 aa） Fragment：UNP residues 123-480	Non-standard monomer：Yes (specific site not provided by mmCIF)	MN MANGANESE (II) ION × 2 PGE TRIETHYLENE GLYCOL × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 7.5；277 K；12.5% PEG3350, 0.1 M HEPES-HCl, 0.2 M ammonium acetate	Resolution 2.12 Å R-free 0.241
6NPZ Crystal structure of Akt1 (aa 123-480) kinase with a bisubstrate Deposited 2019-01-18	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 123–480（358 aa） Fragment：UNP residues 123-480	Non-standard monomer：Yes (specific site not provided by mmCIF)	MN MANGANESE (II) ION × 2 GOL GLYCEROL × 1 VO4 VANADATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 7.5；277 K；12.5% PEG3350, 0.1 M HEPES-HCl, 0.2 M ammonium acetate	Resolution 2.12 Å R-free 0.241
6S9W Crystal Structure of AKT1 in Complex with Covalent-Allosteric AKT Inhibitor 16a Deposited 2019-07-15	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 2–446（445 aa）	Not recorded	L1Z ~{N}-[3-[1-[[4-(5-methyl-6-oxidanylidene-3-phenyl-1~{H}-pyrazin-2-yl)phenyl]methyl]piperidin-4-yl]-2-oxidanylidene-1~{H}-benzimidazol-5-yl]propanamide × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；293 K；1.25 mM Na-acetate, 3.75 mM Na-citrate, 24% v/v PEG 2000 MME, pH 7.0, 3 mg/mL Akt1 (in 25 mM TRIS, 100 mM NaCl, 10% v/v Glycerol, 5 mM DTT, pH 7.5), 1 uL reservoir + 1 uL protein solution	Resolution 2.30 Å R-free 0.263
6S9X Crystal Structure of AKT1 in Complex with Covalent-Allosteric AKT Inhibitor 15c Deposited 2019-07-15	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 2–446（445 aa）	Not recorded	L1W ~{N}-[3-[1-[[4-[5-[(4-hydroxyphenyl)methyl]-6-oxidanylidene-2-phenyl-1~{H}-pyrazin-3-yl]phenyl]methyl]piperidin-4-yl]-2-oxidanylidene-1~{H}-benzimidazol-5-yl]propanamide × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；293 K；1.25 mM Na-acetate, 3.75 mM Na-citrate, 15% v/v PEG 2000 MME, pH 7.5, 3 mg/mL Akt1 (in 25 mM TRIS, 100 mM NaCl, 10% v/v Glycerol, 5 mM DTT, pH 7.5), 1 uL reservoir + 1 uL protein solution	Resolution 2.60 Å R-free 0.234
7APJ Structure of autoinhibited Akt1 reveals mechanism of PIP3-mediated activation Deposited 2020-10-16	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 1–119（119 aa） Chain A 134–445（312 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5；295 K；200 mM malonate, pH 5.0, 16% PEG 3350	Resolution 2.05 Å R-free 0.252
7MYX Crystal structure of the PH domain (R86A) of Akt1 Deposited 2021-05-22	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–121（121 aa） Fragment：PH domain, UNP residues 1-121	Mutation：R86A	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 7.5；298 K；1.28 M Sodium Citrate, 0.1 M Hepes pH 7.5, 0.01 M Praseodymium(III) Acetate	Resolution 1.39 Å R-free 0.204
7NH4 Co-Crystal Structure of Akt1 in Complex with Covalent-Allosteric Akt Inhibitor 3 Deposited 2021-02-10	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 2–446（445 aa）	Mutation：E114A, E115A, E116A	UCE ~{N}-[3-[1-[[4-[5-(hydroxymethyl)-3-phenyl-pyridin-2-yl]phenyl]methyl]piperidin-4-yl]-2-oxidanylidene-1~{H}-benzimidazol-5-yl]propanamide × 1 ACT ACETATE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；293 K；1.25 mM Na-acetate, 3.75 mM Na-citrate, 12% v/v PEG 2000 MME, pH 6.5, 3 mg/mL Akt1 (in 25 mM TRIS, 100 mM NaCl, 10% v/v Glycerol, 5 mM DTT, pH 7.5), 1 uL reservoir + 1 uL protein solution	Resolution 2.30 Å R-free 0.246
7NH5 Co-Crystal Structure of Akt1 in Complex with Covalent-Allosteric Akt Inhibitor 6 Deposited 2021-02-10	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 2–446（445 aa）	Mutation：E114A, E115A, E116A	ACT ACETATE ION × 1 UC8 ~{N}-methyl-6-[4-[[4-[2-oxidanylidene-6-(propanoylamino)-3~{H}-benzimidazol-1-yl]piperidin-1-yl]methyl]phenyl]-5-phenyl-pyridine-3-carboxamide × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；293 K；1.25 mM Na-acetate, 3.75 mM Na-citrate, 18% v/v PEG 2000 MME, pH 6.5, 3 mg/mL Akt1 (in 25 mM TRIS, 100 mM NaCl, 10% v/v Glycerol, 5 mM DTT, pH 7.5), 1 uL reservoir + 1 uL protein solution	Resolution 1.90 Å R-free 0.228
8UVY Structure of AKT1(E17K) with compound 3 Deposited 2023-11-05	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 2–446（445 aa）	Mutation：E17K	EDO 1,2-ETHANEDIOL × 1 XOO 4-{2-[({4-[(2P)-2-(2-aminopyridin-3-yl)-5-phenyl-3H-imidazo[4,5-b]pyridin-3-yl]phenyl}methyl)amino]ethyl}-2-hydroxybenzaldehyde × 1 SO4 SULFATE ION × 6 ZN ZINC ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；298 K；29% PEG3350, 200 mM Li2SO4, 100 mM BisTris Propane pH 8.5, 10% ethylene glycol	Resolution 2.11 Å R-free 0.255
8UW2 Structure of AKT1(E17K) with compound 3 (zinc-free) Deposited 2023-11-05	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 2–446（445 aa）	Not recorded	EDO 1,2-ETHANEDIOL × 2 XOO 4-{2-[({4-[(2P)-2-(2-aminopyridin-3-yl)-5-phenyl-3H-imidazo[4,5-b]pyridin-3-yl]phenyl}methyl)amino]ethyl}-2-hydroxybenzaldehyde × 1 SO4 SULFATE ION × 6	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；298 K；19% PEG3350, 200 mM Li2SO4, 100 mM BisTris Propane pH 8.5, 10% ethylene glycol	Resolution 2.20 Å R-free 0.279
8UW7 Structure of AKT1(WT) with compound 3 Deposited 2023-11-06	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 2–446（445 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF)	EDO 1,2-ETHANEDIOL × 4 XOO 4-{2-[({4-[(2P)-2-(2-aminopyridin-3-yl)-5-phenyl-3H-imidazo[4,5-b]pyridin-3-yl]phenyl}methyl)amino]ethyl}-2-hydroxybenzaldehyde × 1 SO4 SULFATE ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.2；298 K；19% PEG3350, 200 mM Na2SO4, 100 mM BisTris Propane pH 7.2, 10% ethylene glycol	Resolution 1.97 Å R-free 0.265
8UW9 Structure of AKT1(E17K) with compound 4 Deposited 2023-11-06	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 2–446（445 aa）	Not recorded	XQ2 N-({4-[(2P)-2-(2-aminopyridin-3-yl)-5-phenyl-3H-imidazo[4,5-b]pyridin-3-yl]phenyl}methyl)-2-(2-fluoro-4-formyl-3-hydroxyphenyl)acetamide × 1 EDO 1,2-ETHANEDIOL × 3 SO4 SULFATE ION × 4 ZN ZINC ION × 1 CL CHLORIDE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；298 K；15% PEG3350, 200 mM Li2SO4, 100 mM BisTris Propane pH 6.5, 10% ethylene glycol	Resolution 1.90 Å R-free 0.245
9ZBK mTORC2 in complex with Akt1 Deposited 2025-11-20	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric	Chain E 141–478（338 aa）	Not recorded	ZN ZINC ION × 1 A1AID (1M,9M)-1-{4-[4-(prop-2-enoyl)piperazin-1-yl]-3-(trifluoromethyl)phenyl}-9-(quinolin-3-yl)benzo[h][1,6]naphthyridin-2(1H)-one × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.60 Å

37 other PDB entries and 40 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	AKT1_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 5–341； UniProt 144–480 Author chain B； PDBConstruct 5–341； UniProt 144–480

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

SAXS scattering curve SAXS Profile

P(r) Distance Distribution P(r) Distribution

Download Download SAXS (.dat) P(r) (.pr.out) CIF

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	3ow4
Deposition date deposition_date	2010-09-17
Structure title title	Discovery of dihydrothieno- and dihydrofuropyrimidines as potent pan Akt inhibitors
Keywords keywords	SERINE-THREONINE KINASE, TRANSFERASE, TRANSFERASE-TRANSFERASE inhibitor complex; TRANSFERASE/TRANSFERASE inhibitor
Experimental Method method	X-RAY DIFFRACTION

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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier	30.45 Å
Radius of gyration Rg (electron density) rg_electron	29.58 Å
Forward intensity I(0) i0	92693600.00
Molecular weight molecular_weight	77032.0 kDa
Excluded volume excluded_volume	96850 Å³
Envelope volume envelope_volume	121680 Å³
Hydration-shell volume shell_volume	34177 Å³
Envelope diameter envelope_diameter	95.7 Å
Shell Rg shell_rg	37.03 Å
Envelope Rg envelope_rg	29.16 Å
Shape Rg shape_rg	29.56 Å
Total Rg total_rg	30.36 Å
Total atoms total_atoms	5426
Residues n_residues	654
Spherical-harmonic order n_harmonics	20
q range q_range	— – 0.5000 Å⁻¹
Data points n_points	101
Shell type shell_type	directional
Solvent electron density solvent_density	0.3340 e/Å³
Shell contrast contrast_shell	0.0300 e/Å³
CRYSOL version crysol_version	4.1.3

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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax	95.9 Å
Rg (real space) rg_real	30.41 Å
Rg uncertainty (real space) rg_real_error	0.70 Å
I(0) (real space) i0_real	9.2690e+07
I(0) uncertainty (real space) i0_real_error	1.4010e+06
Rg (reciprocal space) rg_reciprocal	30.43 Å
I(0) (reciprocal space) i0_reciprocal	92690000.0000
Solution quality estimate total_estimate	0.9036
Solution quality rating solution_quality	EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks	1
Primary peak position r_peak_primary	94.0 Å
Skewness Skewness skewness	0.223
Kurtosis Kurtosis kurtosis	-0.700
Angular range angular_range	— – 0.2600 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	31830000.0000
Real-space data points n_real_points	53
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.940; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.983; Smooth: 0.939

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (4)

Entity 1 Entity 1 polymer

Description description	RAC-alpha serine/threonine-protein kinase
Molecular weight formula_weight	39467.0 kDa
EC 编号 ec_number	2.7.11.1
Mutation mutation	S473D
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B
Atom count atom_count	5597

GAMARVTMNEFEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVAHTLTENRVLQNSRHPFLTALKYSFQTHDRLCFVMEYANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHSEKNVVYRDLKLENLMLDKDGHIKITDFGLCKEGIKDGATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEEIRFPRTLGPEAKSLLSGLLKKDPKQRLGGGSEDAKEIMQHRFFAGIVWQHVYEKKLSPPFKPQVTSETDTRYFDEEFTAQMITITPPDQDDSMECVDSERRPHFPQFDYSASSTA

来源 Source

来源生物 organism	Homo sapiens
通用名 common_name	human
NCBI Class编号 ncbi_taxonomy_id	9606
宿主生物 host_organism	Spodoptera frugiperda

Entity 2 Entity 2 polymer

Description description	GSK 3 beta peptide
Molecular weight formula_weight	1123.2 kDa
Source method src_method	syn
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	C,D

GRPRTTSFAE

Entity 3 Entity 3 non-polymer

Description description	(2R)-3-(1H-indol-3-yl)-1-{4-[(5S)-5-methyl-5,7-dihydrothieno[3,4-d]pyrimidin-4-yl]piperazin-1-yl}-1-oxopropan-2-amine
Molecular weight formula_weight	422.5 kDa
Source method src_method	syn
Copy count entity_count	2

Entity 4 Entity 4 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	171

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7. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (2 domains)

Domain ID domain_id	d3ow4a_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.144 — Protein kinase-like (PK-like)
Superfamily Superfamily superfamily	d.144.1 — Protein kinase-like (PK-like)
Family Family family	d.144.1.7 — Protein kinases, catalytic subunit

Domain ID domain_id	d3ow4b_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.144 — Protein kinase-like (PK-like)
Superfamily Superfamily superfamily	d.144.1 — Protein kinase-like (PK-like)
Family Family family	d.144.1.7 — Protein kinases, catalytic subunit

CATH v4.4 (4 domains)

Domain ID domain_id	3ow4A01
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	200 — Phosphorylase Kinase; domain 1
Homologous superfamily homologous superfamily	20 — Phosphorylase Kinase; domain 1

Domain ID domain_id	3ow4A02
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	510 — Transferase(Phosphotransferase); domain 1
Homologous superfamily homologous superfamily	10 — Transferase(Phosphotransferase) domain 1

Domain ID domain_id	3ow4B01
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	200 — Phosphorylase Kinase; domain 1
Homologous superfamily homologous superfamily	20 — Phosphorylase Kinase; domain 1

Domain ID domain_id	3ow4B02
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	510 — Transferase(Phosphotransferase); domain 1
Homologous superfamily homologous superfamily	10 — Transferase(Phosphotransferase) domain 1

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8. Citations (1)

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Unit-cell length a length_a	86.427 Å
Unit-cell length b length_b	55.823 Å
Unit-cell length c length_c	91.354 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	103.93 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	4

Space group space_group	P 1 21 1
Space-group number int_tables_number	4
Crystal system crystal_system	—

Resolution resolution	2.600 Å
Low-resolution limit resolution_low	27.470 Å
R factor r_factor	0.1969
R_work r_work	0.1933
R_free r_free	0.2676

fit	/app/data/saxs_computation/ow/3ow4/3ow4.fit
pddf	/app/data/pr_computation/ow/3ow4/3ow4.pr.out
profile	/app/data/saxs_computation/ow/3ow4/3ow4.dat

Discovery of dihydrothieno- and dihydrofuropyrimidines as potent pan Akt inhibitors

1. Protein Identity and Related Structures Protein Identity & Related Structures

RAC-alpha serine/threonine-protein kinase

State in the Current Structure

Other States of the Same Protein in the Database

SAXS scattering curve SAXS Profile

P(r) Distance Distribution P(r) Distribution

2. Structure Basics 2. Structure Basics

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

5. Crystallography and Experiment 5. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

Diffraction experiment Diffraction

6. Entities and Polymers Entities & Polymers (4)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

Entity 2 Entity 2 polymer

Polymer Polymer

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 water

7. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (2 domains)

CATH v4.4 (4 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)