SAXSdb — 6i0m

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

;Inosine-5'-monophosphate dehydrogenase 2 ;

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 homooligomer Homooligomer Protein × 8 PDB declaration: octameric（8） Consistent with protein copy count	Chain A； UniProt 1–514 Chain B； UniProt 1–514	Not recorded	5GP GUANOSINE-5'-MONOPHOSPHATE × 8 GDP GUANOSINE-5'-DIPHOSPHATE × 24 SO4 SULFATE ION × 40	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, SITTING DROP；295 K；0.1 M sodium citrate, pH 5.5 0.2 M lithium sulphate 15% (v/v) ethanol	Resolution 2.57 Å R-free 0.249

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 6I0M	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1B3O TERNARY COMPLEX OF HUMAN TYPE-II INOSINE MONOPHOSPHATE DEHYDROGENASE WITH 6-CL-IMP AND SELENAZOLE ADENINE DINUCLEOTIDE Deposited 1998-12-14	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–514（514 aa）	Not recorded	CPR 6-CHLOROPURINE RIBOSIDE, 5'-MONOPHOSPHATE × 4 SAE SELENAZOLE-4-CARBOXYAMIDE-ADENINE DINUCLEOTIDE × 4	X-RAY DIFFRACTION X-ray crystallization conditions pH 8；SEE PRIMARY REFERENCE , pH 8.0	Resolution 2.90 Å R-free 0.270
1B3O TERNARY COMPLEX OF HUMAN TYPE-II INOSINE MONOPHOSPHATE DEHYDROGENASE WITH 6-CL-IMP AND SELENAZOLE ADENINE DINUCLEOTIDE Deposited 1998-12-14	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain B 1–514（514 aa）	Not recorded	CPR 6-CHLOROPURINE RIBOSIDE, 5'-MONOPHOSPHATE × 4 SAE SELENAZOLE-4-CARBOXYAMIDE-ADENINE DINUCLEOTIDE × 4 UNX UNKNOWN LIGAND × 60	X-RAY DIFFRACTION X-ray crystallization conditions pH 8；SEE PRIMARY REFERENCE , pH 8.0	Resolution 2.90 Å R-free 0.270
1NF7 Ternary complex of the human type II Inosine Monophosphate Dedhydrogenase with Ribavirin Monophosphate and C2-Mycophenolic Adenine Dinucleotide Deposited 2002-12-13	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–514（514 aa）	Not recorded	K POTASSIUM ION × 4 RVP RIBAVIRIN MONOPHOSPHATE × 4 MYD {[5-(6-AMINO-PURIN-7-YL)-3,4-DIHYDROXY-TETRAHYDRO-FURAN-2-YLMETHOXY]-HYDROXY-PHOSPHORYLMETHYL}-PHOSPHONIC ACID MONO-[2-(4-HYDROXY-6-METHOXY-7-METHYL-3-OXO-1,3-DIHYDRO-ISOBENZOFURAN-5-YL)-ETHYL] ESTER × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；277 K；6% PEG 6000, 0.1M Tris-HCl, 24mM beta-mercaptoethanol, 1M LiCl, 10% Glycerol, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 277.0K	Resolution 2.65 Å R-free 0.277
1NF7 Ternary complex of the human type II Inosine Monophosphate Dedhydrogenase with Ribavirin Monophosphate and C2-Mycophenolic Adenine Dinucleotide Deposited 2002-12-13	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain B 1–514（514 aa）	Not recorded	K POTASSIUM ION × 4 RVP RIBAVIRIN MONOPHOSPHATE × 4 MYD {[5-(6-AMINO-PURIN-7-YL)-3,4-DIHYDROXY-TETRAHYDRO-FURAN-2-YLMETHOXY]-HYDROXY-PHOSPHORYLMETHYL}-PHOSPHONIC ACID MONO-[2-(4-HYDROXY-6-METHOXY-7-METHYL-3-OXO-1,3-DIHYDRO-ISOBENZOFURAN-5-YL)-ETHYL] ESTER × 4 UNL UNKNOWN LIGAND × 44	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；277 K；6% PEG 6000, 0.1M Tris-HCl, 24mM beta-mercaptoethanol, 1M LiCl, 10% Glycerol, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 277.0K	Resolution 2.65 Å R-free 0.277
1NFB Ternary complex of the human type II Inosine Monophosphate Dedhydrogenase with 6Cl-IMP and NAD Deposited 2002-12-13	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–514（514 aa）	Not recorded	CPR 6-CHLOROPURINE RIBOSIDE, 5'-MONOPHOSPHATE × 4 NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；277 K；8% PEG 6000, 0.1M Tris-HCl, 24mM beta-mercaptoethanol, 1M LiCl, 20% Glycerol, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 277.0K	Resolution 2.90 Å R-free 0.274
1NFB Ternary complex of the human type II Inosine Monophosphate Dedhydrogenase with 6Cl-IMP and NAD Deposited 2002-12-13	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain B 1–514（514 aa）	Not recorded	CPR 6-CHLOROPURINE RIBOSIDE, 5'-MONOPHOSPHATE × 4 NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；277 K；8% PEG 6000, 0.1M Tris-HCl, 24mM beta-mercaptoethanol, 1M LiCl, 20% Glycerol, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 277.0K	Resolution 2.90 Å R-free 0.274
6I0O Structure of human IMP dehydrogenase, isoform 2, bound to GTP Deposited 2018-10-26	Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 8 PDB declaration: octameric	Chain A 1–514（514 aa） Chain B 1–514（514 aa）	Not recorded	GTP GUANOSINE-5'-TRIPHOSPHATE × 24 SO4 SULFATE ION × 104	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；295 K；25% (w/v) PEG-1500 0.1 M Buffer MIB (malonic acid, imadazole, boric acid), pH 9.0	Resolution 2.62 Å R-free 0.244
6U8E Human IMPDH2 treated with ATP, IMP, and NAD+. Filament assembly interface reconstruction. Deposited 2019-09-04	Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 8 PDB declaration: octameric	Chain A 1–514（514 aa） Chain B 1–514（514 aa） Chain C 1–514（514 aa） Chain D 1–514（514 aa） Chain E 1–514（514 aa） Chain F 1–514（514 aa） Chain G 1–514（514 aa） Chain H 1–514（514 aa）	Not recorded	IMP INOSINIC ACID × 8 NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE × 8	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.03 Å
6U8N Human IMPDH2 treated with ATP, IMP, and NAD+. Fully extended filament segment reconstruction. Deposited 2019-09-05	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 16 PDB declaration: hexadecameric	Chain A 1–514（514 aa） Chain B 1–514（514 aa） Chain C 1–514（514 aa） Chain D 1–514（514 aa） Chain E 1–514（514 aa） Chain F 1–514（514 aa） Chain G 1–514（514 aa） Chain H 1–514（514 aa） Chain I 1–514（514 aa） Chain J 1–514（514 aa） Chain K 1–514（514 aa） Chain L 1–514（514 aa） Chain M 1–514（514 aa） Chain N 1–514（514 aa） Chain O 1–514（514 aa） Chain P 1–514（514 aa）	Not recorded	ATP ADENOSINE-5'-TRIPHOSPHATE × 16 IMP INOSINIC ACID × 8 NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE × 8	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.29 Å
6U8R Human IMPDH2 treated with ATP, IMP, and NAD+. Bent (1/4 compressed, 3/4 extended) segment reconstruction. Deposited 2019-09-05	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 16 PDB declaration: hexadecameric	Chain A 1–514（514 aa） Chain B 1–514（514 aa） Chain C 1–514（514 aa） Chain D 1–514（514 aa） Chain E 1–514（514 aa） Chain F 1–514（514 aa） Chain G 1–514（514 aa） Chain H 1–514（514 aa） Chain I 1–514（514 aa） Chain J 1–514（514 aa） Chain K 1–514（514 aa） Chain L 1–514（514 aa） Chain M 1–514（514 aa） Chain N 1–514（514 aa） Chain O 1–514（514 aa） Chain P 1–514（514 aa）	Not recorded	IMP INOSINIC ACID × 8 NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE × 8 ATP ADENOSINE-5'-TRIPHOSPHATE × 16	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.91 Å
6U8S Human IMPDH2 treated with ATP, IMP, NAD+, and 2 mM GTP. Filament assembly interface reconstruction. Deposited 2019-09-05	Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 8 PDB declaration: octameric	Chain A 1–514（514 aa） Chain B 1–514（514 aa） Chain C 1–514（514 aa） Chain D 1–514（514 aa） Chain E 1–514（514 aa） Chain F 1–514（514 aa） Chain G 1–514（514 aa） Chain H 1–514（514 aa）	Not recorded	IMP INOSINIC ACID × 8 NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE × 8	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.14 Å
6U9O Human IMPDH2 treated with ATP, IMP, NAD+, and 2 mM GTP. Fully compressed filament segment reconstruction. Deposited 2019-09-09	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 16 PDB declaration: hexadecameric	Chain A 1–514（514 aa） Chain B 1–514（514 aa） Chain C 1–514（514 aa） Chain D 1–514（514 aa） Chain E 1–514（514 aa） Chain F 1–514（514 aa） Chain G 1–514（514 aa） Chain H 1–514（514 aa） Chain I 1–514（514 aa） Chain J 1–514（514 aa） Chain K 1–514（514 aa） Chain L 1–514（514 aa） Chain M 1–514（514 aa） Chain N 1–514（514 aa） Chain O 1–514（514 aa） Chain P 1–514（514 aa）	Not recorded	GTP GUANOSINE-5'-TRIPHOSPHATE × 16 ATP ADENOSINE-5'-TRIPHOSPHATE × 8 IMP INOSINIC ACID × 8 NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE × 8	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.36 Å
6UA2 Human IMPDH2 treated with ATP, IMP, NAD+, and 2 mM GTP. Bent (2/4 compressed, 2/4 extended) segment reconstruction. Deposited 2019-09-10	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 16 PDB declaration: hexadecameric	Chain A 1–514（514 aa） Chain B 1–514（514 aa） Chain C 1–514（514 aa） Chain D 1–514（514 aa） Chain E 1–514（514 aa） Chain F 1–514（514 aa） Chain G 1–514（514 aa） Chain H 1–514（514 aa） Chain I 1–514（514 aa） Chain J 1–514（514 aa） Chain K 1–514（514 aa） Chain L 1–514（514 aa） Chain M 1–514（514 aa） Chain N 1–514（514 aa） Chain O 1–514（514 aa） Chain P 1–514（514 aa）	Not recorded	GTP GUANOSINE-5'-TRIPHOSPHATE × 8 ATP ADENOSINE-5'-TRIPHOSPHATE × 12 IMP INOSINIC ACID × 8 NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE × 8	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 4.20 Å
6UA4 Human IMPDH2 treated with ATP, IMP, NAD+, and 2 mM GTP. Bent (3/4 compressed, 1/4 extended) segment reconstruction. Deposited 2019-09-10	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 16 PDB declaration: hexadecameric	Chain A 1–514（514 aa） Chain B 1–514（514 aa） Chain C 1–514（514 aa） Chain D 1–514（514 aa） Chain E 1–514（514 aa） Chain F 1–514（514 aa） Chain G 1–514（514 aa） Chain H 1–514（514 aa） Chain I 1–514（514 aa） Chain J 1–514（514 aa） Chain K 1–514（514 aa） Chain L 1–514（514 aa） Chain M 1–514（514 aa） Chain N 1–514（514 aa） Chain O 1–514（514 aa） Chain P 1–514（514 aa）	Not recorded	GTP GUANOSINE-5'-TRIPHOSPHATE × 12 ATP ADENOSINE-5'-TRIPHOSPHATE × 10 IMP INOSINIC ACID × 8 NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE × 8	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.65 Å
6UA5 Human IMPDH2 treated with ATP, IMP, NAD+, and 2 mM GTP. Free interfacial octamer reconstruction. Deposited 2019-09-10	Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 8 PDB declaration: octameric	Chain A 1–514（514 aa） Chain B 1–514（514 aa） Chain C 1–514（514 aa） Chain D 1–514（514 aa） Chain E 1–514（514 aa） Chain F 1–514（514 aa） Chain G 1–514（514 aa） Chain H 1–514（514 aa）	Not recorded	IMP INOSINIC ACID × 8 NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE × 8	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.79 Å
6UAJ Human IMPDH2 treated with ATP, IMP, NAD+, and 2 mM GTP. Free canonical octamer reconstruction. Deposited 2019-09-10	Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 8 PDB declaration: octameric	Chain A 1–514（514 aa） Chain B 1–514（514 aa） Chain C 1–514（514 aa） Chain D 1–514（514 aa） Chain E 1–514（514 aa） Chain F 1–514（514 aa） Chain G 1–514（514 aa） Chain H 1–514（514 aa）	Not recorded	GTP GUANOSINE-5'-TRIPHOSPHATE × 16 ATP ADENOSINE-5'-TRIPHOSPHATE × 8 IMP INOSINIC ACID × 8 NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE × 8	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.84 Å
6UC2 Human IMPDH2 treated with ATP and 2 mM GTP. Free canonical octamer reconstruction. Deposited 2019-09-13	Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 8 PDB declaration: octameric	Chain A 1–514（514 aa） Chain B 1–514（514 aa） Chain C 1–514（514 aa） Chain D 1–514（514 aa） Chain E 1–514（514 aa） Chain F 1–514（514 aa） Chain G 1–514（514 aa） Chain H 1–514（514 aa）	Not recorded	GTP GUANOSINE-5'-TRIPHOSPHATE × 16 ATP ADENOSINE-5'-TRIPHOSPHATE × 8	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 4.48 Å
6UDO Human IMPDH2 treated with ATP, IMP, and 20 mM GTP. Fully compressed filament segment reconstruction. Deposited 2019-09-19	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 16 PDB declaration: hexadecameric	Chain A 1–514（514 aa） Chain B 1–514（514 aa） Chain C 1–514（514 aa） Chain D 1–514（514 aa） Chain E 1–514（514 aa） Chain F 1–514（514 aa） Chain G 1–514（514 aa） Chain H 1–514（514 aa） Chain I 1–514（514 aa） Chain J 1–514（514 aa） Chain K 1–514（514 aa） Chain L 1–514（514 aa） Chain M 1–514（514 aa） Chain N 1–514（514 aa） Chain O 1–514（514 aa） Chain P 1–514（514 aa）	Not recorded	IMP INOSINIC ACID × 8 GTP GUANOSINE-5'-TRIPHOSPHATE × 16 ATP ADENOSINE-5'-TRIPHOSPHATE × 8	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.21 Å
6UDP Human IMPDH2 treated with ATP, IMP, and 20 mM GTP. Filament assembly interface reconstruction. Deposited 2019-09-19	Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 8 PDB declaration: octameric	Chain A 1–514（514 aa） Chain B 1–514（514 aa） Chain C 1–514（514 aa） Chain D 1–514（514 aa） Chain E 1–514（514 aa） Chain F 1–514（514 aa） Chain G 1–514（514 aa） Chain H 1–514（514 aa）	Not recorded	IMP INOSINIC ACID × 8	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.95 Å
6UDQ Human IMPDH2 treated with ATP, IMP, and 20 mM GTP. Fully compressed filament end reconstruction. Deposited 2019-09-19	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 12 PDB declaration: dodecameric	Chain A 1–514（514 aa） Chain B 1–514（514 aa） Chain C 1–514（514 aa） Chain D 1–514（514 aa） Chain E 1–514（514 aa） Chain F 1–514（514 aa） Chain G 1–514（514 aa） Chain H 1–514（514 aa） Chain I 1–514（514 aa） Chain J 1–514（514 aa） Chain K 1–514（514 aa） Chain L 1–514（514 aa）	Not recorded	IMP INOSINIC ACID × 8 GTP GUANOSINE-5'-TRIPHOSPHATE × 16 ATP ADENOSINE-5'-TRIPHOSPHATE × 8	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.27 Å
8FOZ Human IMPDH2 mutant - L245P, treated with ATP, IMP, and NAD+; filament assembly interface reconstruction Deposited 2023-01-03	Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 8 PDB declaration: octameric	Chain A 1–514（514 aa） Chain B 1–514（514 aa） Chain C 1–514（514 aa） Chain D 1–514（514 aa） Chain E 1–514（514 aa） Chain F 1–514（514 aa） Chain G 1–514（514 aa） Chain H 1–514（514 aa）	Mutation：L245P Mutation：L245P Mutation：L245P Mutation：L245P Mutation：L245P Mutation：L245P Mutation：L245P Mutation：L245P	IMP INOSINIC ACID × 8 NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE × 8	ELECTRON MICROSCOPY cryo-EM buffer pH 7 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.00 Å
8FUZ Human IMPDH2 mutant - L245P, treated with GTP, ATP, IMP, and NAD+; filament assembly interface reconstruction Deposited 2023-01-18	Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 8 PDB declaration: octameric	Chain A 1–514（514 aa） Chain B 1–514（514 aa） Chain C 1–514（514 aa） Chain D 1–514（514 aa） Chain E 1–514（514 aa） Chain F 1–514（514 aa） Chain G 1–514（514 aa） Chain H 1–514（514 aa）	Mutation：L245P Mutation：L245P Mutation：L245P Mutation：L245P Mutation：L245P Mutation：L245P Mutation：L245P Mutation：L245P	IMP INOSINIC ACID × 8 NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE × 8	ELECTRON MICROSCOPY cryo-EM buffer pH 7 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.10 Å
8G8F Human IMPDH2 mutant - L245P, treated with ATP, IMP, and NAD+; extended filament segment reconstruction Deposited 2023-02-17	Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 8 PDB declaration: octameric	Chain A 1–514（514 aa） Chain B 1–514（514 aa） Chain C 1–514（514 aa） Chain D 1–514（514 aa） Chain E 1–514（514 aa） Chain F 1–514（514 aa） Chain G 1–514（514 aa） Chain H 1–514（514 aa）	Mutation：L245P Mutation：L245P Mutation：L245P Mutation：L245P Mutation：L245P Mutation：L245P Mutation：L245P Mutation：L245P	ATP ADENOSINE-5'-TRIPHOSPHATE × 16 IMP INOSINIC ACID × 8 NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE × 8	ELECTRON MICROSCOPY cryo-EM buffer pH 7 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.60 Å
8G9B Human IMPDH2 mutant - L245P, treated with GTP, ATP, IMP, and NAD+; compressed filament segment reconstruction Deposited 2023-02-21	Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 8 PDB declaration: octameric	Chain A 1–514（514 aa） Chain B 1–514（514 aa） Chain C 1–514（514 aa） Chain D 1–514（514 aa） Chain E 1–514（514 aa） Chain F 1–514（514 aa） Chain G 1–514（514 aa） Chain H 1–514（514 aa）	Mutation：L245P Mutation：L245P Mutation：L245P Mutation：L245P Mutation：L245P Mutation：L245P Mutation：L245P Mutation：L245P	GTP GUANOSINE-5'-TRIPHOSPHATE × 16 ATP ADENOSINE-5'-TRIPHOSPHATE × 8 IMP INOSINIC ACID × 8 NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE × 8	ELECTRON MICROSCOPY cryo-EM buffer pH 7 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.00 Å
9DMU Cryo-EM structure of IMPDH2 bound to IMP and GAD Deposited 2024-09-14	Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 8 PDB declaration: octameric	Chain A 1–514（514 aa） Chain B 1–514（514 aa） Chain C 1–514（514 aa） Chain D 1–514（514 aa） Chain E 1–514（514 aa） Chain F 1–514（514 aa） Chain G 1–514（514 aa） Chain H 1–514（514 aa）	Not recorded	IMP INOSINIC ACID × 8 A1A7T [[(2~{R},3~{S},4~{R},5~{R})-5-(6-aminopurin-9-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methoxy-oxidanyl-phosphoryl] [(2~{R},3~{S},4~{R},5~{R})-3,4-bis(oxidanyl)-5-[3-(thiophen-2-ylcarbonylamino)pyridin-1-yl]oxolan-2-yl]methyl hydrogen phosphate × 8 K POTASSIUM ION × 8	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 1.82 Å
9MUB Human IMPDH2 mutant - S160del, treated with GTP, ATP, IMP, and NAD+; tetramer reconstruction Deposited 2025-01-13	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–514（514 aa） Chain B 1–514（514 aa） Chain C 1–514（514 aa） Chain D 1–514（514 aa）	Mutation：S160del Mutation：S160del Mutation：S160del Mutation：S160del	IMP INOSINIC ACID × 4 NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE × 4	ELECTRON MICROSCOPY cryo-EM buffer pH 7 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.50 Å
9MUC Human IMPDH2 mutant - S160del, treated with GTP, ATP, IMP, and NAD+; interfacial octamer reconstruction Deposited 2025-01-13	Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 8 PDB declaration: octameric	Chain A 1–514（514 aa） Chain B 1–514（514 aa） Chain C 1–514（514 aa） Chain D 1–514（514 aa） Chain E 1–514（514 aa） Chain F 1–514（514 aa） Chain G 1–514（514 aa） Chain H 1–514（514 aa）	Mutation：S160del Mutation：S160del Mutation：S160del Mutation：S160del Mutation：S160del Mutation：S160del Mutation：S160del Mutation：S160del	IMP INOSINIC ACID × 8 NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE × 8	ELECTRON MICROSCOPY cryo-EM buffer pH 7 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.10 Å

24 other PDB entries and 27 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	IMDH2_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 4–517； UniProt 1–514 Author chain B； PDBConstruct 4–517； UniProt 1–514

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.

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	6i0m
Deposition date deposition_date	2018-10-26
Structure title title	Structure of human IMP dehydrogenase, isoform 2, bound to GDP
Keywords keywords	oxidoreductase, de novo guanine nucleotide biosynthesis, BIOSYNTHETIC PROTEIN; BIOSYNTHETIC PROTEIN
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	33.40 Å
Radius of gyration Rg (electron density) rg_electron	32.92 Å
Forward intensity I(0) i0	156412000.00
Molecular weight molecular_weight	95811.0 kDa
Excluded volume excluded_volume	118190 Å³
Envelope volume envelope_volume	159730 Å³
Hydration-shell volume shell_volume	40129 Å³
Envelope diameter envelope_diameter	112.4 Å
Shell Rg shell_rg	40.18 Å
Envelope Rg envelope_rg	32.50 Å
Shape Rg shape_rg	32.94 Å
Total Rg total_rg	33.41 Å
Total atoms total_atoms	12977
Residues n_residues	894
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	102.6 Å
Rg (real space) rg_real	33.28 Å
Rg uncertainty (real space) rg_real_error	0.61 Å
I(0) (real space) i0_real	1.5640e+08
I(0) uncertainty (real space) i0_real_error	2.5050e+06
Rg (reciprocal space) rg_reciprocal	33.36 Å
I(0) (reciprocal space) i0_reciprocal	156400000.0000
Solution quality estimate total_estimate	0.9130
Solution quality rating solution_quality	EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	39.3 Å
Skewness Skewness skewness	0.090
Kurtosis Kurtosis kurtosis	-0.745
Angular range angular_range	— – 0.2350 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	23170000.0000
Real-space data points n_real_points	48
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.966; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.998; Smooth: 0.968

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (5)

Entity 1 Entity 1 polymer

Description description	;Inosine-5'-monophosphate dehydrogenase 2 ;
Molecular weight formula_weight	56157.1 kDa
EC 编号 ec_number	1.1.1.205
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	13153

GSHMADYLISGGTSYVPDDGLTAQQLFNCGDGLTYNDFLILPGYIDFTADQVDLTSALTKKITLKTPLVSSPMDTVTEAGMAIAMALTGGIGFIHHNCTPEFQANEVRKVKKYEQGFITDPVVLSPKDRVRDVFEAKARHGFCGIPITDTGRMGSRLVGIISSRDIDFLKEEEHDCFLEEIMTKREDLVVAPAGITLKEANEILQRSKKGKLPIVNEDDELVAIIARTDLKKNRDYPLASKDAKKQLLCGAAIGTHEDDKYRLDLLAQAGVDVVVLDSSQGNSIFQINMIKYIKDKYPNLQVIGGNVVTAAQAKNLIDAGVDALRVGMGSGSICITQEVLACGRPQATAVYKVSEYARRFGVPVIADGGIQNVGHIAKALALGASTVMMGSLLAATTEAPGEYFFSDGIRLKKYRGMGSLDAMDKHLSSQNRYFSEADKIKVAQGVSGAVQDKGSIHKFVPYLIAGIQHSCQDIGAKSLTQVRAMMYSGELKFEKRTSSAQVEGGVHSLHSYEKRLF

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	Escherichia coli BL21(DE3)

Entity 2 Entity 2 non-polymer

Description description	GUANOSINE-5'-MONOPHOSPHATE
Molecular weight formula_weight	363.2 kDa
Source method src_method	syn
Copy count entity_count	2

Entity 3 Entity 3 non-polymer

Description description	GUANOSINE-5'-DIPHOSPHATE
Molecular weight formula_weight	443.2 kDa
Source method src_method	syn
Copy count entity_count	6

Entity 4 Entity 4 non-polymer

Description description	SULFATE ION
Molecular weight formula_weight	96.1 kDa
Source method src_method	syn
Copy count entity_count	10

Entity 5 Entity 5 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	74

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7. Fold Classification (SCOP + CATH) 2 domains

CATH v4.4 (2 domains)

Domain ID domain_id	6i0mA00
Class class	3 — Alpha Beta
Architecture architecture	20 — Alpha-Beta Barrel
Topology topology	20 — TIM Barrel
Homologous superfamily homologous superfamily	70 — Aldolase class I

Domain ID domain_id	6i0mB00
Class class	3 — Alpha Beta
Architecture architecture	20 — Alpha-Beta Barrel
Topology topology	20 — TIM Barrel
Homologous superfamily homologous superfamily	70 — Aldolase class I

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8. Citations (1)

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Unit-cell length a length_a	134.729 Å
Unit-cell length b length_b	134.729 Å
Unit-cell length c length_c	324.081 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.00 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	32

Space group space_group	I 4 2 2
Space-group number int_tables_number	97
Crystal system crystal_system	—

Resolution resolution	2.567 Å
Low-resolution limit resolution_low	162.000 Å
R factor r_factor	0.2203
R_work r_work	0.2187
R_free r_free	0.2487

fit	/app/data/saxs_computation/i0/6i0m/6i0m.fit
pddf	/app/data/pr_computation/i0/6i0m/6i0m.pr.out
profile	/app/data/saxs_computation/i0/6i0m/6i0m.dat

Structure of human IMP dehydrogenase, isoform 2, bound to GDP

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

;Inosine-5'-monophosphate dehydrogenase 2 ;

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