UniProt Q6N0W9
Ribulose bisphosphate carboxylase (Q6N0W9)
Ribulose bisphosphate carboxylase (UniProt Q6N0W9), EC 4.1.1.39: 22 experimental structures on GenesisL1, 4 ligands bound, 40 pockets. Binding sites, pockets, druggability and 3D structures in GL1X.
- UniProt
- Q6N0W9
- Protein
- Ribulose bisphosphate carboxylase
- EC
- 4.1.1.39
- Experimental structures
- 22
- Predicted models
- 0
- Ligands
- 4
- Pockets
- 40 · 2 records with a druggable one
Structures
22 records of Q6N0W9 in the MolNFT archive: 22 experimental, 0 predicted.
| Entry | Title | Method | Chains | Ligands | Pockets |
|---|---|---|---|---|---|
| 4LF1 | Hexameric Form II RuBisCO from Rhodopseudomonas palustris, activated and complexed with 2-CABP | x-ray diffraction | A, B, C, D, E, F | — | — |
| 4LF1 | Hexameric form II rubisco from rhodopseudomonas palustris, activated and complexed with 2-cabp | x-ray diffraction | A, B, C, D, E, F | — | — |
| 4LF2 | Hexameric Form II RuBisCO from Rhodopseudomonas palustris, activated and complexed with sulfate and… | x-ray diffraction | A, B, C, D, E, F | — | — |
| 4LF2 | Hexameric form II rubisco from rhodopseudomonas palustris, activated and complexed with sulfate and… | x-ray diffraction | A, B, C, D, E, F | — | — |
| 5HAN | Structure function studies of R. palustris RubisCO (S59F mutant; CABP-bound) | x-ray diffraction | A, B, C, D, E, F, G, H, I, J, K, L | CAP, MG | 20 (best 0.83) |
| 5HAN | Structure function studies of R. palustris rubisco (S59F mutant; cabp- bound) | x-ray diffraction | A, B, C, D, E, F, G, H, I, J, K, L | — | — |
| 5HAO | Structure function studies of R. palustris RubisCO (M331A mutant; CABP-bound) | x-ray diffraction | A, B, C, D, E, F | CAP, MG | — |
| 5HAO | Structure function studies of R. palustris rubisco (M331A mutant; cabp-bound) | x-ray diffraction | A, B, C, D, E, F | — | — |
| 5HAT | Structure function studies of R. palustris RubisCO (S59F/M331A mutant; CABP-bound) | x-ray diffraction | A, B, C, D, E, F, G, H, I, J, K, L | CAP, MG | — |
| 5HAT | Structure function studies of R. palustris rubisco (S59F/M331A mutant; cabp-bound) | x-ray diffraction | A, B, C, D, E, F, G, H, I, J, K, L | — | — |
| 5HJX | Structure function studies of R. palustris RubisCO (A47V mutant; CABP-bound) | x-ray diffraction | A, B, C, D, E, F | CAP, MG | — |
| 5HJX | Structure function studies of R. palustris rubisco (A47V mutant; cabp- bound) | x-ray diffraction | A, B, C, D, E, F | — | — |
| 5HJY | Structure function studies of R. palustris RubisCO (I165T mutant; CABP-bound) | x-ray diffraction | A, B, C, D, E, F | CAP, MG, CL | — |
| 5HJY | Structure function studies of R. palustris rubisco (I165T mutant; cabp-bound) | x-ray diffraction | A, B, C, D, E, F | — | — |
| 5HK4 | Structure function studies of R. palustris RubisCO (A47V-M331A mutant) | x-ray diffraction | A, B, C, D, E, F | CAP, MG | — |
| 5HK4 | Structure function studies of R. palustris rubisco (A47V-M331A mutant) | x-ray diffraction | A, B, C, D, E, F | — | — |
| 5HQL | Structure function studies of R. palustris RubisCO (A47V-M331A mutant; CABP-bound; no expression… | x-ray diffraction | A, B, C, D, E, F | CAP, MG | — |
| 5HQL | Structure function studies of R. palustris rubisco (A47V-M331A mutant; cabp-bound; no expression… | x-ray diffraction | A, B, C, D, E, F | — | — |
| 5HQM | Structure function studies of R. palustris rubisco (R. PALUSTRIS/R. rubrum chimera) | x-ray diffraction | A, B | — | — |
| 5KOZ | Structure function studies of R. palustris RubisCO (K192C mutant; CABP-bound) | x-ray diffraction | A, B, C, D, E, F, G, H, I, J, K, L | CAP, MG, CO3 | 20 (best 0.84) |
| 5KOZ | Structure function studies of R. palustris rubisco (K192C mutant; cabp-bound) | x-ray diffraction | A, B, C, D, E, F, G, H, I, J, K, L | CAP, MG, CO3 | — |
| Q6N0W9 | AlphaFold monomer V2.0 prediction for ribulose bisphosphate carboxylase (Q6N0W9) | — | — | — |
Ligands
Experiment against prediction
- 5HQM chain B against the predicted model P04718: TM-score 0.99, RMSD 0.60 Å
- 5HQM chain A against the predicted model P04718: TM-score 0.99, RMSD 0.63 Å
Elsewhere
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