UniProt A0A4V3YUQ9
Phospholipid ABC transporter ATP-binding protein MlaF (A0A4V3YUQ9)
Phospholipid ABC transporter ATP-binding protein MlaF (UniProt A0A4V3YUQ9): 10 experimental structures on GenesisL1, 2 ligands bound, 64 pockets. Binding sites, pockets, druggability and 3D structures in GL1X.
- UniProt
- A0A4V3YUQ9
- Protein
- Phospholipid ABC transporter ATP-binding protein MlaF
- Experimental structures
- 10
- Predicted models
- 0
- Ligands
- 2
- Pockets
- 64 · 6 records with a druggable one
Structures
10 records of A0A4V3YUQ9 in the MolNFT archive: 10 experimental, 0 predicted.
| Entry | Title | Method | Chains | Ligands | Pockets |
|---|---|---|---|---|---|
| 7CGE | The overall structure of nucleotide free MlaFEDB complex | electron microscopy | B, E | — | 11 (best 0.70) |
| 7CGE | The overall structure of nucleotide free mlafedb complex | electron microscopy | B, E | — | — |
| 7CGN | The overall structure of the MlaFEDB complex in ATP-bound EQtall conformation (Mutation of E170Q on… | electron microscopy | B, E | ATP | 7 (best 0.69) |
| 7CGN | The overall structure of the mlafedb complex in ATP-bound eqtall conformation (mutation of E170Q on… | electron microscopy | B, E | ATP | — |
| 7CH0 | The overall structure of the MlaFEDB complex in ATP-bound EQclose conformation (Mutation of E170Q… | electron microscopy | B, E | ATP | 9 (best 0.82) |
| 7CH0 | The overall structure of the mlafedb complex in ATP-bound eqclose conformation (mutation of E170Q… | electron microscopy | B, E | ATP | — |
| 7CH6 | Cryo-EM structure of E.coli MlaFEB with AMPPNP | electron microscopy | C, D | ANP | 12 (best 0.67) |
| 7CH6 | Cryo-EM structure of E.COLI mlafeb with amppnp | electron microscopy | C, D | ANP | 12 (best 0.67) |
| 7CH7 | Cryo-EM structure of E.coli MlaFEB | electron microscopy | C, D | — | 13 (best 0.67) |
| 7CH7 | Cryo-EM structure of E.COLI mlafeb | electron microscopy | C, D | — | — |
Ligands
Elsewhere
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.