UniProt A0A0F7R8C5
A0A0F7R8C5
A0A0F7R8C5 (UniProt A0A0F7R8C5): 7 experimental structures on GenesisL1, 2 ligands bound. Binding sites, pockets, druggability and 3D structures in GL1X.
- UniProt
- A0A0F7R8C5
- Experimental structures
- 7
- Predicted models
- 0
- Ligands
- 2
Structures
7 records of A0A0F7R8C5 in the MolNFT archive: 7 experimental, 0 predicted.
| Entry | Title | Method | Chains | Ligands | Pockets |
|---|---|---|---|---|---|
| 5IAT | Mechanistic and Structural Analysis of Substrate Recognition and Cofactor Binding by an Unusual… | x-ray diffraction | A, B | — | — |
| 5IAT | Mechanistic and structural analysis of substrate recognition and cofactor binding by an unusual… | x-ray diffraction | A, B | — | — |
| 5IAV | Mechanistic and Structural Analysis of Substrate Recognition and Cofactor Binding by an Unusual… | x-ray diffraction | A, B | CO | — |
| 5IAV | Mechanistic and structural analysis of substrate recognition and cofactor binding by an unusual… | x-ray diffraction | A, B | — | — |
| 5IAX | Mechanistic and Structural Analysis of Substrate Recognition and Cofactor Binding by an Unusual… | x-ray diffraction | A, B | CO, AKG | — |
| 5IAX | Mechanistic and structural analysis of substrate recognition and cofactor binding by an unusual… | x-ray diffraction | A, B | — | — |
| 5V7Y | Prolyl 4-hydroxylase interacts with and modifies elongation factor tu | x-ray diffraction | A, B, D, C | CO, AKG | — |
Ligands
Elsewhere
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