UniProt O97725
NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 12 (O97725)
NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 12 (UniProt O97725): 56 experimental structures and 1 predicted model on GenesisL1, 4 ligands bound, 65 pockets. Binding sites, druggability and experiment against…
- UniProt
- O97725
- Protein
- NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 12
- Experimental structures
- 56
- Predicted models
- 1
- Ligands
- 4
- Pockets
- 65 · 36 records with a druggable one
Structures
57 records of O97725 in the MolNFT archive: 56 experimental, 1 predicted.
| Entry | Title | Method | Chains | Ligands | Pockets |
|---|---|---|---|---|---|
| 5LC5 | Structure of mammalian respiratory Complex I, class2 | electron microscopy | q | — | 2 (best 0.84) |
| 5LC5 | Structure of mammalian respiratory complex I, CLASS2 | electron microscopy | q | — | — |
| 5LDW | Structure of mammalian respiratory Complex I, class1 | electron microscopy | q | — | — |
| 5LDW | Structure of mammalian respiratory complex I, CLASS1 | electron microscopy | q | — | — |
| 5LDX | Structure of mammalian respiratory Complex I, class3. | electron microscopy | q | — | 2 (best 0.88) |
| 5LDX | Structure of mammalian respiratory complex I, CLASS3. | electron microscopy | q | — | — |
| 5O31 | Mitochondrial complex I in the deactive state | electron microscopy | q | — | 4 (best 0.87) |
| 5O31 | Mitochondrial complex I in the deactive state | electron microscopy | q | — | — |
| 7DGQ | Activity optimized supercomplex state1 | electron microscopy | U | CDL | — |
| 7DGR | Activity optimized supercomplex state2 | electron microscopy | U | CDL | 1 (best 0.84) |
| 7DGS | Activity optimized supercomplex state3 | electron microscopy | U | CDL | — |
| 7DGZ | Activity optimized complex I (closed form) | electron microscopy | U | CDL | — |
| 7DGZ | Activity optimized complex I (closed form) | electron microscopy | U | CDL | — |
| 7DH0 | Activity optimized complex I (open form) | electron microscopy | U | — | 1 (best 0.83) |
| 7DH0 | Activity optimized complex I (open form) | electron microscopy | U | — | — |
| 7DKF | Activity optimized supercomplex state4 | electron microscopy | U2 | — | — |
| 7QSD | Bovine complex I in the active state at 3.1 A | electron microscopy | q | PC1, CDL | 1 (best 0.84) |
| 7QSD | Bovine complex I in the active state at 3.1 a | electron microscopy | q | PC1, CDL | — |
| 7QSK | Bovine complex I in lipid nanodisc, Active-Q10 | electron microscopy | q | PC1, CDL | 1 (best 0.85) |
| 7QSK | Bovine complex I in lipid nanodisc, active-Q10 | electron microscopy | q | PC1, CDL | — |
| 7QSL | Bovine complex I in lipid nanodisc, Active-apo | electron microscopy | q | PC1, CDL | 2 (best 0.84) |
| 7QSL | Bovine complex I in lipid nanodisc, active-apo | electron microscopy | q | PC1, CDL | — |
| 7QSM | Bovine complex I in lipid nanodisc, Deactive-ligand (composite) | electron microscopy | q | PC1, CDL | 1 (best 0.84) |
| 7QSM | Bovine complex I in lipid nanodisc, deactive-ligand (composite) | electron microscopy | q | PC1, CDL | — |
| 7QSN | Bovine complex I in lipid nanodisc, Deactive-apo | electron microscopy | q | PC1, CDL | 2 (best 0.84) |
| 7QSN | Bovine complex I in lipid nanodisc, deactive-apo | electron microscopy | q | PC1, CDL | — |
| 7QSO | Bovine complex I in lipid nanodisc, State 3 (Slack) | electron microscopy | q | PC1, CDL | — |
| 7QSO | Bovine complex I in lipid nanodisc, state 3 (slack) | electron microscopy | q | PC1, CDL | — |
| 7R41 | Bovine complex I in the presence of IM1761092, active class i (Composite map) | electron microscopy | q | PC1, CDL | 1 (best 0.85) |
| 7R42 | Bovine complex I in the presence of IM1761092, active class ii (Composite map) | electron microscopy | q | PC1, CDL | 2 (best 0.84) |
| 7R43 | Bovine complex I in the presence of IM1761092, active class iii (Composite map) | electron microscopy | q | PC1, CDL | — |
| 7R44 | Bovine complex I in the presence of IM1761092, active class iv (Composite map) | electron microscopy | q | PC1, CDL | 2 (best 0.84) |
| 7R45 | Bovine complex I in the presence of IM1761092, deactive class i (Composite map) | electron microscopy | q | PC1, CDL | 2 (best 0.84) |
| 7R46 | Bovine complex I in the presence of IM1761092, deactive class ii (Composite map) | electron microscopy | q | PC1, CDL | 2 (best 0.84) |
| 7R47 | Bovine complex I in the presence of IM1761092, deactive class iii (Composite map) | electron microscopy | q | PC1, CDL | — |
| 7R48 | Bovine complex I in the presence of IM1761092, deactive class iv (Composite map) | electron microscopy | q | PC1, CDL | 2 (best 0.83) |
| 7R4C | Bovine complex I in the presence of IM1761092, deactive class v (Composite map) | electron microscopy | q | PC1, CDL | 2 (best 0.84) |
| 7R4D | Bovine complex I in the presence of IM1761092, deactive class vi (Composite map) | electron microscopy | q | PC1, CDL | 2 (best 0.84) |
| 7R4F | Bovine complex I in the presence of IM1761092, slack class i (Composite map) | electron microscopy | q | PC1, CDL | 2 (best 0.84) |
| 7R4G | Bovine complex I in the presence of IM1761092, slack class ii (Composite map) | electron microscopy | q | PC1, CDL | 2 (best 0.84) |
| 8Q0A | Inward-facing, closed proteoliposome complex I at 3.1 A. Initially purified in DDM. | electron microscopy | q | PC1, 3PE, CDL | 1 (best 0.84) |
| 8Q0F | Inward-facing, open2 proteoliposome complex I at 3.1 A. Initially purified in DDM. | electron microscopy | q | PLC, CDL, PC1 | 2 (best 0.83) |
| 8Q0J | Inward-facing, slack proteoliposome complex I at 3.8 A. Initially purified in DDM. | electron microscopy | q | PC1, CDL | 1 (best 0.84) |
| 8Q0M | Outward-facing, closed proteoliposome complex I at 3.1 A. Initially purified in DDM. | electron microscopy | q | PC1, 3PE, CDL | 2 (best 0.83) |
| 8Q0O | Outward-facing, open2 proteoliposome complex I at 3.1 A. Initially purified in DDM. | electron microscopy | q | PC1, 3PE, CDL | 2 (best 0.83) |
| 8Q0Q | Outward-facing, slack proteoliposome complex I at 3.6 A. Initially purified in DDM | electron microscopy | q | PC1, CDL | 2 (best 0.83) |
| 8Q1P | Inward-facing, open2 proteoliposome complex I at 2.9 A, after deactivation treatment. Initially… | electron microscopy | q | PC1, PLC, CDL | 2 (best 0.83) |
| 8Q1U | Inward-facing, open1 proteoliposome complex I at 3.3 A, after deactivation treatment. Initially… | electron microscopy | q | PLC, CDL, PC1 | 1 (best 0.82) |
| 8Q1Y | Outward-facing, open2 proteoliposome complex I at 2.6 A, after deactivation treatment. Initially… | electron microscopy | q | PC1, 3PE, CDL | 1 (best 0.84) |
| 8Q25 | Outward-facing, open1 proteoliposome complex I at 2.8 A, after deactivation treatment. Initially… | electron microscopy | q | PC1, 3PE, CDL | 2 (best 0.84) |
| 8Q45 | Inward-facing, closed proteoliposome complex I at 2.7 A. Initially purified in LMNG. | electron microscopy | q | PC1, CDL, 3PE | 1 (best 0.84) |
| 8Q46 | Inward-facing, open2 proteoliposome complex I at 2.6 A. Initially purified in LMNG. | electron microscopy | q | PLC, CDL, PC1 | 2 (best 0.83) |
| 8Q47 | Inward-facing, open1 proteoliposome complex I at 2.9 A. Initially purified in LMNG. | electron microscopy | q | PLC, PC1, CDL | 2 (best 0.84) |
| 8Q48 | Outward-facing, closed proteoliposome complex I at 2.5 A. Initially purified in LMNG. | electron microscopy | q | PC1, 3PE, CDL | 2 (best 0.83) |
| 8Q49 | Outward-facing, open2 proteoliposome complex I at 2.6 A. Initially purified in LMNG. | electron microscopy | q | PC1, 3PE, CDL | 2 (best 0.84) |
| 8Q4A | Outward-facing, open1 proteoliposome complex I at 2.6 A. Initially purified in LMNG. | electron microscopy | q | PC1, 3PE, CDL | 2 (best 0.84) |
| O97725 | AlphaFold monomer V2.0 prediction for NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 12… | predicted | A | — | 2 (best 0.47) |
Ligands
Experiment against prediction
- 7R4F chain q against the predicted model O97725: TM-score 0.92, RMSD 1.39 Å
- 7R4G chain q against the predicted model O97725: TM-score 0.92, RMSD 1.40 Å
- 7R43 chain q against the predicted model O97725: TM-score 0.92, RMSD 1.44 Å
- 7R44 chain q against the predicted model O97725: TM-score 0.92, RMSD 1.42 Å
- 7QSD chain q against the predicted model O97725: TM-score 0.92, RMSD 1.41 Å
- 7QSD chain q against the predicted model O97725: TM-score 0.92, RMSD 1.41 Å
- 7R41 chain q against the predicted model O97725: TM-score 0.92, RMSD 1.43 Å
- 7R42 chain q against the predicted model O97725: TM-score 0.92, RMSD 1.43 Å
- 7R4C chain q against the predicted model O97725: TM-score 0.92, RMSD 1.44 Å
- 7R46 chain q against the predicted model O97725: TM-score 0.92, RMSD 1.46 Å
Elsewhere
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