UniProt P03902
NADH-ubiquinone oxidoreductase chain 4L (P03902)
NADH-ubiquinone oxidoreductase chain 4L (UniProt P03902), EC 1.6.5.3, 7.1.1.2: 35 experimental structures and 1 predicted model on GenesisL1, 2 ligands bound, 34 pockets. Binding sites, druggability and experiment against…
- UniProt
- P03902
- Protein
- NADH-ubiquinone oxidoreductase chain 4L
- EC
- 1.6.5.3, 7.1.1.2
- Experimental structures
- 35
- Predicted models
- 1
- Ligands
- 2
- Pockets
- 34 · 19 records with a druggable one
Structures
36 records of P03902 in the MolNFT archive: 35 experimental, 1 predicted.
| Entry | Title | Method | Chains | Ligands | Pockets |
|---|---|---|---|---|---|
| 5LC5 | Structure of mammalian respiratory complex I, CLASS2 | electron microscopy | K | — | — |
| 5LDW | Structure of mammalian respiratory Complex I, class1 | electron microscopy | K | — | — |
| 5LDW | Structure of mammalian respiratory complex I, CLASS1 | electron microscopy | K | — | — |
| 5LDX | Structure of mammalian respiratory complex I, CLASS3. | electron microscopy | K | — | — |
| 5O31 | Mitochondrial complex I in the deactive state | electron microscopy | K | — | 1 (best 0.88) |
| 5O31 | Mitochondrial complex I in the deactive state | electron microscopy | K | — | — |
| 7DGQ | Activity optimized supercomplex state1 | electron microscopy | 5 | — | 2 (best 0.85) |
| 7DGZ | Activity optimized complex I (closed form) | electron microscopy | 5 | — | — |
| 7DH0 | Activity optimized complex I (open form) | electron microscopy | 5 | — | — |
| 7DKF | Activity optimized supercomplex state4 | electron microscopy | 52 | — | 1 (best 0.88) |
| 7QSD | Bovine complex I in the active state at 3.1 A | electron microscopy | K | 3PE | 2 (best 0.86) |
| 7QSD | Bovine complex I in the active state at 3.1 a | electron microscopy | K | 3PE | — |
| 7QSK | Bovine complex I in lipid nanodisc, active-Q10 | electron microscopy | K | 3PE | — |
| 7QSL | Bovine complex I in lipid nanodisc, active-apo | electron microscopy | K | CDL | — |
| 7QSM | Bovine complex I in lipid nanodisc, Deactive-ligand (composite) | electron microscopy | K | 3PE | 2 (best 0.86) |
| 7QSM | Bovine complex I in lipid nanodisc, deactive-ligand (composite) | electron microscopy | K | 3PE | — |
| 7QSN | Bovine complex I in lipid nanodisc, deactive-apo | electron microscopy | K | 3PE | — |
| 7QSO | Bovine complex I in lipid nanodisc, State 3 (Slack) | electron microscopy | K | — | — |
| 7QSO | Bovine complex I in lipid nanodisc, state 3 (slack) | electron microscopy | K | — | — |
| 7R41 | Bovine complex I in the presence of IM1761092, active class i (Composite map) | electron microscopy | K | CDL | 2 (best 0.86) |
| 7R43 | Bovine complex I in the presence of IM1761092, active class iii (Composite map) | electron microscopy | K | CDL | — |
| 7R44 | Bovine complex I in the presence of IM1761092, active class iv (Composite map) | electron microscopy | K | CDL | 1 (best 0.90) |
| 7R45 | Bovine complex I in the presence of IM1761092, deactive class i (Composite map) | electron microscopy | K | CDL | 2 (best 0.86) |
| 7R46 | Bovine complex I in the presence of IM1761092, deactive class ii (Composite map) | electron microscopy | K | CDL | 2 (best 0.89) |
| 7R47 | Bovine complex I in the presence of IM1761092, deactive class iii (Composite map) | electron microscopy | K | CDL | — |
| 7R48 | Bovine complex I in the presence of IM1761092, deactive class iv (Composite map) | electron microscopy | K | CDL | 1 (best 0.89) |
| 7R4C | Bovine complex I in the presence of IM1761092, deactive class v (Composite map) | electron microscopy | K | CDL | 2 (best 0.86) |
| 7R4G | Bovine complex I in the presence of IM1761092, slack class ii (Composite map) | electron microscopy | K | — | 2 (best 0.88) |
| 8Q0A | Inward-facing, closed proteoliposome complex I at 3.1 A. Initially purified in DDM. | electron microscopy | K | 3PE | 2 (best 0.85) |
| 8Q0J | Inward-facing, slack proteoliposome complex I at 3.8 A. Initially purified in DDM. | electron microscopy | K | — | 3 (best 0.90) |
| 8Q0M | Outward-facing, closed proteoliposome complex I at 3.1 A. Initially purified in DDM. | electron microscopy | K | 3PE | 2 (best 0.86) |
| 8Q1P | Inward-facing, open2 proteoliposome complex I at 2.9 A, after deactivation treatment. Initially… | electron microscopy | K | 3PE | 1 (best 0.90) |
| 8Q1U | Inward-facing, open1 proteoliposome complex I at 3.3 A, after deactivation treatment. Initially… | electron microscopy | K | 3PE | 2 (best 0.86) |
| 8Q1Y | Outward-facing, open2 proteoliposome complex I at 2.6 A, after deactivation treatment. Initially… | electron microscopy | K | 3PE | 2 (best 0.86) |
| 8Q4A | Outward-facing, open1 proteoliposome complex I at 2.6 A. Initially purified in LMNG. | electron microscopy | K | 3PE | 2 (best 0.87) |
| P03902 | AlphaFold monomer V2.0 prediction for NADH-ubiquinone oxidoreductase chain 4L (P03902) | predicted | A | — | — |
Ligands
Experiment against prediction
- 7QSK chain K against the predicted model P03902: TM-score 0.98, RMSD 0.47 Å
- 7QSM chain K against the predicted model P03902: TM-score 0.98, RMSD 0.47 Å
- 7QSM chain K against the predicted model P03902: TM-score 0.98, RMSD 0.47 Å
- 7R44 chain K against the predicted model P03902: TM-score 0.98, RMSD 0.48 Å
- 7R41 chain K against the predicted model P03902: TM-score 0.98, RMSD 0.49 Å
- 7R43 chain K against the predicted model P03902: TM-score 0.98, RMSD 0.49 Å
- 7R47 chain K against the predicted model P03902: TM-score 0.98, RMSD 0.49 Å
- 7QSN chain K against the predicted model P03902: TM-score 0.98, RMSD 0.49 Å
- 7R48 chain K against the predicted model P03902: TM-score 0.98, RMSD 0.49 Å
- 7R4C chain K against the predicted model P03902: TM-score 0.98, RMSD 0.49 Å
Elsewhere
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