6u8n

Human IMPDH2 treated with ATP, IMP, and NAD+. Fully extended filament segment reconstruction.

Method: ELECTRON MICROSCOPY D_max: 144.1 Å Quality: GOOD

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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 × 16 PDB declaration: hexadecameric（16） Consistent with protein copy count	Chain A； UniProt 1–514 Chain B； UniProt 1–514 Chain C； UniProt 1–514 Chain D； UniProt 1–514 Chain E； UniProt 1–514 Chain F； UniProt 1–514 Chain G； UniProt 1–514 Chain H； UniProt 1–514 Chain I； UniProt 1–514 Chain J； UniProt 1–514 Chain K； UniProt 1–514 Chain L； UniProt 1–514 Chain M； UniProt 1–514 Chain N； UniProt 1–514 Chain O； UniProt 1–514 Chain P； UniProt 1–514	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

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 6U8N	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 method 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 method 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 method 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 method 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 method 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 method 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
6I0M Structure of human IMP dehydrogenase, isoform 2, bound to GDP Deposited 2018-10-26	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 × 8 PDB declaration: octameric	Chain A 1–514（514 aa） Chain B 1–514（514 aa）	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
6I0O Structure of human IMP dehydrogenase, isoform 2, bound to GTP Deposited 2018-10-26	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 × 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 oligomeric state Different ligand/ion 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
6U8R Human IMPDH2 treated with ATP, IMP, and NAD+. Bent (1/4 compressed, 3/4 extended) segment reconstruction. Deposited 2019-09-05	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 oligomeric state Different ligand/ion 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 ligand/ion 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 ligand/ion 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 ligand/ion 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 oligomeric state Different ligand/ion 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 oligomeric state Different ligand/ion 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 oligomeric state Different ligand/ion 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 ligand/ion 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 oligomeric state Different ligand/ion 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 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 oligomeric state 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） 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 oligomeric state 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） 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 oligomeric state 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 oligomeric state 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） 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 oligomeric state 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） 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 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 oligomeric state 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） 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 6–519； UniProt 1–514 Author chain B； PDBConstruct 6–519； UniProt 1–514 Author chain C； PDBConstruct 6–519； UniProt 1–514 Author chain D； PDBConstruct 6–519； UniProt 1–514 Author chain E； PDBConstruct 6–519； UniProt 1–514 Author chain F； PDBConstruct 6–519； UniProt 1–514 Author chain G； PDBConstruct 6–519； UniProt 1–514 Author chain H； PDBConstruct 6–519； UniProt 1–514 Author chain I； PDBConstruct 6–519； UniProt 1–514 Author chain J； PDBConstruct 6–519； UniProt 1–514 Author chain K； PDBConstruct 6–519； UniProt 1–514 Author chain L； PDBConstruct 6–519； UniProt 1–514 Author chain M； PDBConstruct 6–519； UniProt 1–514 Author chain N； PDBConstruct 6–519； UniProt 1–514 Author chain O； PDBConstruct 6–519； UniProt 1–514 Author chain P； PDBConstruct 6–519； 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.

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	6u8n
Deposition date deposition_date	2019-09-05
Structure title title	Human IMPDH2 treated with ATP, IMP, and NAD+. Fully extended filament segment reconstruction.
Keywords keywords	metabolism, filament, allostery, adenine, guanine, BIOSYNTHETIC PROTEIN; BIOSYNTHETIC PROTEIN
Experimental Method method	ELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier	52.98 Å
Radius of gyration Rg (electron density) rg_electron	52.48 Å
Forward intensity I(0) i0	3034820000.00
Molecular weight molecular_weight	450950.0 kDa
Excluded volume excluded_volume	560060 Å³
Envelope volume envelope_volume	850720 Å³
Hydration-shell volume shell_volume	127230 Å³
Envelope diameter envelope_diameter	152.2 Å
Shell Rg shell_rg	64.02 Å
Envelope Rg envelope_rg	49.80 Å
Shape Rg shape_rg	52.49 Å
Total Rg total_rg	52.75 Å
Total atoms total_atoms	31528
Residues n_residues	4016
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	144.1 Å
Rg (real space) rg_real	52.56 Å
Rg uncertainty (real space) rg_real_error	0.55 Å
I(0) (real space) i0_real	3.0350e+09
I(0) uncertainty (real space) i0_real_error	4.6610e+07
Rg (reciprocal space) rg_reciprocal	53.32 Å
I(0) (reciprocal space) i0_reciprocal	3038000000.0000
Solution quality estimate total_estimate	0.8416
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	1
Primary peak position r_peak_primary	76.9 Å
Skewness Skewness skewness	-0.189
Kurtosis Kurtosis kurtosis	-0.598
Angular range angular_range	— – 0.1500 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	150500000.0000
Real-space data points n_real_points	31
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.952; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.080

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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	;Inosine-5'-monophosphate dehydrogenase 2 ;
Molecular weight formula_weight	56480.5 kDa
EC 编号 ec_number	1.1.1.205
Source method src_method	man
Copy count entity_count	16

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	I,A,J,B,K,C,L,D,M,E,N,F,O,G,P,H
Atom count atom_count	31528

SEFELMADYLISGGTSYVPDDGLTAQQLFNCGDGLTYNDFLILPGYIDFTADQVDLTSALTKKITLKTPLVSSPMDTVTEAGMAIAMALTGGIGFIHHNCTPEFQANEVRKVKKYEQGFITDPVVLSPKDRVRDVFEAKARHGFCGIPITDTGRMGSRLVGIISSRDIDFLKEEEHDCFLEEIMTKREDLVVAPAGITLKEANEILQRSKKGKLPIVNEDDELVAIIARTDLKKNRDYPLASKDAKKQLLCGAAIGTHEDDKYRLDLLAQAGVDVVVLDSSQGNSIFQINMIKYIKDKYPNLQVIGGNVVTAAQAKNLIDAGVDALRVGMGSGSICITQEVLACGRPQATAVYKVSEYARRFGVPVIADGGIQNVGHIAKALALGASTVMMGSLLAATTEAPGEYFFSDGIRLKKYRGMGSLDAMDKHLSSQNRYFSEADKIKVAQGVSGAVQDKGSIHKFVPYLIAGIQHSCQDIGAKSLTQVRAMMYSGELKFEKRTSSAQVEGGVHSLHSYEKRLF

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

Entity 2 Entity 2 non-polymer

Description description	ADENOSINE-5'-TRIPHOSPHATE
Molecular weight formula_weight	507.2 kDa
Source method src_method	syn
Copy count entity_count	16

Entity 3 Entity 3 non-polymer

Description description	INOSINIC ACID
Molecular weight formula_weight	348.2 kDa
Source method src_method	syn
Copy count entity_count	8

Entity 4 Entity 4 non-polymer

Description description	NICOTINAMIDE-ADENINE-DINUCLEOTIDE
Molecular weight formula_weight	663.4 kDa
Source method src_method	syn
Copy count entity_count	8

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8. Citations (1)

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Unit-cell length a length_a	1.000 Å
Unit-cell length b length_b	1.000 Å
Unit-cell length c length_c	1.000 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	—

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

Resolution resolution	3.29 Å
Resolution测定方法 resolution_method	—
颗粒数 num_particles	9124

fit	/app/data/saxs_computation/u8/6u8n/6u8n.fit
pddf	/app/data/pr_computation/u8/6u8n/6u8n.pr.out
profile	/app/data/saxs_computation/u8/6u8n/6u8n.dat