UniProt A0A0U1MUE2
Phosphodiesterase acting on cyclic dinucleotides (A0A0U1MUE2)
Phosphodiesterase acting on cyclic dinucleotides (UniProt A0A0U1MUE2): 8 experimental structures on GenesisL1, 5 ligands bound, 7 pockets. Binding sites, pockets, druggability and 3D structures in GL1X.
- UniProt
- A0A0U1MUE2
- Protein
- Phosphodiesterase acting on cyclic dinucleotides
- Experimental structures
- 8
- Predicted models
- 0
- Ligands
- 5
- Pockets
- 7 · 4 records with a druggable one
Structures
8 records of A0A0U1MUE2 in the MolNFT archive: 8 experimental, 0 predicted.
| Entry | Title | Method | Chains | Ligands | Pockets |
|---|---|---|---|---|---|
| 5XSI | The catalytic domain of GdpP | x-ray diffraction | A, B | MN | 2 (best 0.76) |
| 5XSI | The catalytic domain of gdpp | x-ray diffraction | A, B | MN | — |
| 5XSN | The catalytic domain of GdpP with c-di-AMP | x-ray diffraction | A, B | MN, 2BA | 2 (best 0.75) |
| 5XSN | The catalytic domain of gdpp with C-di-AMP | x-ray diffraction | A, B | MN, 2BA | — |
| 5XSP | The catalytic domain of GdpP with 5'-pApA | x-ray diffraction | A, B | MN, AMP | 2 (best 0.75) |
| 5XSP | The catalytic domain of gdpp with 5'-papa | x-ray diffraction | A, B | MN, A | — |
| 5XT3 | The catalytic domain of GdpP with c-di-GMP | x-ray diffraction | A, B | MN, C2E | 1 (best 0.74) |
| 5XT3 | The catalytic domain of gdpp with C-di-gmp | x-ray diffraction | A, B | MN, C2E | — |
Ligands
- MN · Manganese (II) ion · in 8 records
- 2BA · (2r,3r,3as,5r,7ar,9r,10r,10as,12r,14ar)-2,9-bis(6-amino-9H-purin-9-yl)octahydro-2H,7H-difuro[3,2-D:3', 2'-J][1,3,7,9,2,8 ]tetraoxadiphosphacyclododecine-3,5, 10,12-tetrol 5,12-dioxide · in 2 records
- C2E · 9,9'-[(2r,3r,3as,5s,7ar,9r,10r,10as,12s,14ar)-3,5,10, 12-tetrahydroxy-5,12-dioxidooctahydro-2H,7H-difuro[3, 2-D:3',2'-J][1,3,7,9,2, 8]tetraoxadiphosphacyclododecine-2,9-diyl]bis(2-amino-1,9-dihydro-6H-purin-6-one) · in 2 records
- A · Adenosine-5'-monophosphate · in 1 record
- AMP · Adenosine monophosphate · in 1 record
Elsewhere
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