UniProt Q9CES5
Glutamine ABC transporter permease and substrate binding protein protein (Q9CES5)
Glutamine ABC transporter permease and substrate binding protein protein (UniProt Q9CES5): 10 experimental structures on GenesisL1, 10 pockets. Binding sites, pockets, druggability and 3D structures in GL1X.
- UniProt
- Q9CES5
- Protein
- Glutamine ABC transporter permease and substrate binding protein protein
- Experimental structures
- 10
- Predicted models
- 0
- Pockets
- 10 · 1 record with a druggable one
Structures
10 records of Q9CES5 in the MolNFT archive: 10 experimental, 0 predicted.
| Entry | Title | Method | Chains | Ligands | Pockets |
|---|---|---|---|---|---|
| 4KPT | Crystal structure of substrate binding domain 1 (SBD1) OF ABC transporter GLNPQ from lactococcus… | x-ray diffraction | A, B | — | — |
| 4KPT | Crystal structure of substrate binding domain 1 (SBD1) of ABC transporter glnpq from lactococcus… | x-ray diffraction | A, B | — | — |
| 4KQP | Crystal structure of Lactococcus lactis GlnP substrate binding domain 2 (SBD2) in complex with… | x-ray diffraction | A | — | — |
| 4KQP | Crystal structure of lactococcus lactis glnp substrate binding domain 2 (SBD2) in complex with… | x-ray diffraction | A | — | — |
| 4KR5 | Crystal structure of Lactococcus lactis GlnP substrate binding domain 2 (SBD2) in open conformation | x-ray diffraction | A, B | — | — |
| 4KR5 | Crystal structure of lactococcus lactis glnp substrate binding domain 2 (SBD2) in open conformation | x-ray diffraction | A, B | — | — |
| 4LA9 | Crystal structure of an empty substrate binding domain 1 (SBD1) OF ABC TRANSPORTER GLNPQ from… | x-ray diffraction | A, B | — | — |
| 4LA9 | Crystal structure of an empty substrate binding domain 1 (SBD1) of ABC transporter glnpq from… | x-ray diffraction | A, B | — | — |
| 6H30 | The crystal structure of SBD1-SBD2 tandem of GlnPQ transporter | x-ray diffraction | A, B | — | 10 (best 0.72) |
| 6H30 | The crystal structure of SBD1-SBD2 tandem of glnpq transporter | x-ray diffraction | A, B | — | — |
Elsewhere
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