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6I0O: 
Structure of human IMP dehydrogenase, isoform 2, bound to GTP
Biological unit 1: octameric
Source organism: Homo sapiens
Number of proteins:
8 (Inosine-5'-monophosphate dehydrogenase 2 ▼)
Protein molecule
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AA -Click to explore this molecule neighborsBB -Click to explore this molecule neighborsA_1A_1 -Click to explore this molecule neighborsA_2A_2 -Click to explore this molecule neighborsA_3A_3 -Click to explore this molecule neighborsB_1B_1 -Click to explore this molecule neighbors
B_2B_2 -Click to explore this molecule neighborsB_3B_3 -Click to explore this molecule neighbors
 Inosine-5'-monophosphate dehydrogenase 2
Number of chemicals:
128 (GUANOSINE-5'-TRIPHOSPHATE (24),SULFATE ION (104) ▼)
Chemical
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GUANOSINE-5'-TRIPHOSPHATE (24)
SULFATE ION (104)
Similar Structures (6361)help
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Showing 1 to 10 out of 6361 selected structures help
      PDB ID Description Taxonomy▲▼ Aligned Protein▲▼ RMSD▲▼ Aligned Residues▲▼ Sequence Identity▲▼
1
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 6UC2
Human IMPDH2 treated with ATP and 2 mM GTP. Free canonical octamer reconstruction
Homo sapiens
 8 1.43Å 3453 100%
2
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 6UA2
Human IMPDH2 treated with ATP, IMP, NAD+, and 2 mM GTP. Bent (2/4 compressed, 2/4 extended) segment reconstruction
Homo sapiens
 8 6.21Å 3440 98%
3
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 6UAJ
Human IMPDH2 treated with ATP, IMP, NAD+, and 2 mM GTP. Free canonical octamer reconstruction
Homo sapiens
 8 1.23Å 3439 100%
4
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 6U9O
Human IMPDH2 treated with ATP, IMP, NAD+, and 2 mM GTP. Fully compressed filament segment reconstruction
Homo sapiens
 8 1.30Å 3435 100%
5
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 6UA4
Human IMPDH2 treated with ATP, IMP, NAD+, and 2 mM GTP. Bent (3/4 compressed, 1/4 extended) segment reconstruction
Homo sapiens
 8 3.38Å 3431 98%
6
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 6UDQ
Human IMPDH2 treated with ATP, IMP, and 20 mM GTP. Fully compressed filament end reconstruction
Homo sapiens
 8 1.07Å 3430 100%
7
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 6RFU
In cellulo crystallization of Trypanosoma brucei IMP dehydrogenase enables the identification of ATP and GMP as genuine co-factors
Trypanosoma brucei brucei
 8 2.39Å 3396 50%
8
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 6I0M
Structure of human IMP dehydrogenase, isoform 2, bound to GDP
Homo sapiens
 8 0.64Å 3360 100%
9
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 4Z87
Structure of the IMP dehydrogenase from Ashbya gossypii bound to GDP
Eremothecium gossypii ATCC 10895
 8 1.70Å 3360 62%
10
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 6JIG
Crystal structure of GMP reductase C318A from Trypanosoma brucei in complex with guanosine 5'-monophosphate
Trypanosoma brucei brucei
 8 2.34Å 3268 35%
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{"1":"Inosine-5'-monophosphate dehydrogenase 2","2":"Inosine-5'-monophosphate dehydrogenase 2","124":"Inosine-5'-monophosphate dehydrogenase 2","125":"Inosine-5'-monophosphate dehydrogenase 2","126":"Inosine-5'-monophosphate dehydrogenase 2","127":"Inosine-5'-monophosphate dehydrogenase 2","128":"Inosine-5'-monophosphate dehydrogenase 2","129":"Inosine-5'-monophosphate dehydrogenase 2"}
Citing VAST
Gibrat JF, Madej T, Bryant SH. "Surprising similarities in structure comparison.", Curr Opin Struct Biol.1996 Jun;6(3):377-85
Madej T, Lanczycki CJ, Zhang D, Thiessen PA, Geer RC, Marchler-Bauer A, Bryant SH. "MMDB and VAST+: tracking structural similarities between macromolecular complexes." Nucl. Acids Res. 2014 Jan;42(Database issue):D297-303
Thomas Madej, Aron Marchler-Bauer, Christopher Lanczycki, Dachuan Zhang, Stephen H Bryant "Biological Assembly Comparison With VAST" Methods Mol. Biol. 2020(2112):175-186
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?Original VAST
Original VAST finds structures that are similar to individual protein molecules, or individual 3D domains, in your query structure. Select a protein molecule ("chain") or 3D domain of interest from the table below to view a list of other proteins or domains that have a similar 3D shape. In contrast to VAST+, which focuses on the default biological unit, Original VAST lists all protein molecules in the asymmetric unit of the query structure.