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Protein Structures and Oligomeric States

Enter a protein name, UniProt accession or PDB ID. Name searches ask you to confirm the protein identity before related structures are queried.

Current Protein Identity：P12268 New Search
25PDB entries
28Biological assembly
218chain/assembly records
Main Difference Dimensions in This Set
Different mutation/modification Different assembly state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics

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

Related-Structure Differences

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

PDB Entry Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Experimental Method Experimental Conditions Structure Quality
1B3O TERNARY COMPLEX OF HUMAN TYPE-II INOSINE MONOPHOSPHATE DEHYDROGENASE WITH 6-CL-IMP AND SELENAZOLE ADENINE DINUCLEOTIDE Deposited 1998-12-14 Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric（4） Consistent with protein count
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 Assembly 2 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric（4） Consistent with protein count
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 Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric（4） Consistent with protein count
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 Assembly 2 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric（4） Consistent with protein count
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 Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric（4） Consistent with protein count
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 Assembly 2 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric（4） Consistent with protein count
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 Assembly 1 Protein homooligomer Homooligomer；Protein × 8 PDB declaration: octameric（8） Consistent with protein count
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 Assembly 1 Protein homooligomer Homooligomer；Protein × 8 PDB declaration: octameric（8） Consistent with protein count
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 Assembly 1 Protein homooligomer Homooligomer；Protein × 8 PDB declaration: octameric（8） Consistent with protein count
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 Assembly 1 Protein homooligomer Homooligomer；Protein × 16 PDB declaration: hexadecameric（16） Consistent with protein count
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 Assembly 1 Protein homooligomer Homooligomer；Protein × 16 PDB declaration: hexadecameric（16） Consistent with protein count
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 Assembly 1 Protein homooligomer Homooligomer；Protein × 8 PDB declaration: octameric（8） Consistent with protein count
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 Assembly 1 Protein homooligomer Homooligomer；Protein × 16 PDB declaration: hexadecameric（16） Consistent with protein count
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 Assembly 1 Protein homooligomer Homooligomer；Protein × 16 PDB declaration: hexadecameric（16） Consistent with protein count
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 Assembly 1 Protein homooligomer Homooligomer；Protein × 16 PDB declaration: hexadecameric（16） Consistent with protein count
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 Assembly 1 Protein homooligomer Homooligomer；Protein × 8 PDB declaration: octameric（8） Consistent with protein count
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 Assembly 1 Protein homooligomer Homooligomer；Protein × 8 PDB declaration: octameric（8） Consistent with protein count
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 Assembly 1 Protein homooligomer Homooligomer；Protein × 8 PDB declaration: octameric（8） Consistent with protein count
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 Assembly 1 Protein homooligomer Homooligomer；Protein × 16 PDB declaration: hexadecameric（16） Consistent with protein count
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 Assembly 1 Protein homooligomer Homooligomer；Protein × 8 PDB declaration: octameric（8） Consistent with protein count
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 Assembly 1 Protein homooligomer Homooligomer；Protein × 12 PDB declaration: dodecameric（12） Consistent with protein count
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 Assembly 1 Protein homooligomer Homooligomer；Protein × 8 PDB declaration: octameric（8） Consistent with protein count
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 Assembly 1 Protein homooligomer Homooligomer；Protein × 8 PDB declaration: octameric（8） Consistent with protein count
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 Assembly 1 Protein homooligomer Homooligomer；Protein × 8 PDB declaration: octameric（8） Consistent with protein count
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 Assembly 1 Protein homooligomer Homooligomer；Protein × 8 PDB declaration: octameric（8） Consistent with protein count
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 Assembly 1 Protein homooligomer Homooligomer；Protein × 8 PDB declaration: octameric（8） Consistent with protein count
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 Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric（4） Consistent with protein count
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 Assembly 1 Protein homooligomer Homooligomer；Protein × 8 PDB declaration: octameric（8） Consistent with protein count
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

This page presents structural evidence recorded in PDB/mmCIF.“No recorded non-water small molecule” does not prove that the experimental sample was ligand-free; experimental conditions belong to the PDB experiment, while ligands and copy counts are shown for each biological assembly.