UniProt P03924
NADH-ubiquinone oxidoreductase chain 6 (P03924)
NADH-ubiquinone oxidoreductase chain 6 (UniProt P03924), EC 1.6.5.3, 7.1.1.2: 55 experimental structures on GenesisL1, 4 ligands bound, 147 pockets. Binding sites, pockets, druggability and 3D structures in GL1X.
- UniProt
- P03924
- Protein
- NADH-ubiquinone oxidoreductase chain 6
- EC
- 1.6.5.3, 7.1.1.2
- Experimental structures
- 55
- Predicted models
- 0
- Ligands
- 4
- Pockets
- 147 · 38 records with a druggable one
Structures
55 records of P03924 in the MolNFT archive: 55 experimental, 0 predicted.
| Entry | Title | Method | Chains | Ligands | Pockets |
|---|---|---|---|---|---|
| 5LC5 | Structure of mammalian respiratory Complex I, class2 | electron microscopy | J | — | 2 (best 0.90) |
| 5LC5 | Structure of mammalian respiratory complex I, CLASS2 | electron microscopy | J | — | — |
| 5LDW | Structure of mammalian respiratory Complex I, class1 | electron microscopy | J | — | — |
| 5LDW | Structure of mammalian respiratory complex I, CLASS1 | electron microscopy | J | — | — |
| 5LDX | Structure of mammalian respiratory Complex I, class3. | electron microscopy | J | — | 2 (best 0.88) |
| 5LDX | Structure of mammalian respiratory complex I, CLASS3. | electron microscopy | J | — | — |
| 5O31 | Mitochondrial complex I in the deactive state | electron microscopy | J | — | 2 (best 0.88) |
| 5O31 | Mitochondrial complex I in the deactive state | electron microscopy | J | — | — |
| 7DGQ | Activity optimized supercomplex state1 | electron microscopy | 7 | 3PE | 3 (best 0.85) |
| 7DGR | Activity optimized supercomplex state2 | electron microscopy | 7 | — | 1 (best 0.88) |
| 7DGZ | Activity optimized complex I (closed form) | electron microscopy | 7 | 3PE | 4 (best 0.89) |
| 7DGZ | Activity optimized complex I (closed form) | electron microscopy | 7 | 3PE | — |
| 7DH0 | Activity optimized complex I (open form) | electron microscopy | 7 | — | 2 (best 0.88) |
| 7DH0 | Activity optimized complex I (open form) | electron microscopy | 7 | — | — |
| 7DKF | Activity optimized supercomplex state4 | electron microscopy | 72 | — | 2 (best 0.89) |
| 7QSD | Bovine complex I in the active state at 3.1 A | electron microscopy | J | 3PE | 5 (best 0.86) |
| 7QSD | Bovine complex I in the active state at 3.1 a | electron microscopy | J | 3PE | — |
| 7QSK | Bovine complex I in lipid nanodisc, Active-Q10 | electron microscopy | J | PC1, CDL, 3PE | 5 (best 0.87) |
| 7QSK | Bovine complex I in lipid nanodisc, active-Q10 | electron microscopy | J | PC1, CDL, 3PE | — |
| 7QSL | Bovine complex I in lipid nanodisc, active-apo | electron microscopy | J | 3PE, CDL, PC1 | — |
| 7QSM | Bovine complex I in lipid nanodisc, Deactive-ligand (composite) | electron microscopy | J | 3PE, PC1 | 5 (best 0.86) |
| 7QSM | Bovine complex I in lipid nanodisc, deactive-ligand (composite) | electron microscopy | J | PC1, 3PE | — |
| 7QSN | Bovine complex I in lipid nanodisc, Deactive-apo | electron microscopy | J | 3PE, PC1 | 4 (best 0.86) |
| 7QSN | Bovine complex I in lipid nanodisc, deactive-apo | electron microscopy | J | 3PE, PC1 | — |
| 7QSO | Bovine complex I in lipid nanodisc, State 3 (Slack) | electron microscopy | J | 3PE, PC1 | — |
| 7QSO | Bovine complex I in lipid nanodisc, state 3 (slack) | electron microscopy | J | 3PE, PC1 | — |
| 7R41 | Bovine complex I in the presence of IM1761092, active class i (Composite map) | electron microscopy | J | 3PE, CDL | 5 (best 0.86) |
| 7R42 | Bovine complex I in the presence of IM1761092, active class ii (Composite map) | electron microscopy | J | 3PE, CDL | 3 (best 0.92) |
| 7R43 | Bovine complex I in the presence of IM1761092, active class iii (Composite map) | electron microscopy | J | 3PE, CDL | — |
| 7R44 | Bovine complex I in the presence of IM1761092, active class iv (Composite map) | electron microscopy | J | 3PE, CDL | 4 (best 0.90) |
| 7R45 | Bovine complex I in the presence of IM1761092, deactive class i (Composite map) | electron microscopy | J | 3PE, CDL | 6 (best 0.86) |
| 7R46 | Bovine complex I in the presence of IM1761092, deactive class ii (Composite map) | electron microscopy | J | CDL, 3PE | 5 (best 0.89) |
| 7R47 | Bovine complex I in the presence of IM1761092, deactive class iii (Composite map) | electron microscopy | J | 3PE, CDL | — |
| 7R48 | Bovine complex I in the presence of IM1761092, deactive class iv (Composite map) | electron microscopy | J | 3PE, CDL | 3 (best 0.89) |
| 7R4C | Bovine complex I in the presence of IM1761092, deactive class v (Composite map) | electron microscopy | J | 3PE, CDL | 5 (best 0.86) |
| 7R4D | Bovine complex I in the presence of IM1761092, deactive class vi (Composite map) | electron microscopy | J | — | 5 (best 0.89) |
| 7R4F | Bovine complex I in the presence of IM1761092, slack class i (Composite map) | electron microscopy | J | 3PE | 2 (best 0.88) |
| 7R4G | Bovine complex I in the presence of IM1761092, slack class ii (Composite map) | electron microscopy | J | 3PE | 3 (best 0.88) |
| 8Q0A | Inward-facing, closed proteoliposome complex I at 3.1 A. Initially purified in DDM. | electron microscopy | J | 3PE, PC1, CDL, PLC | 6 (best 0.86) |
| 8Q0F | Inward-facing, open2 proteoliposome complex I at 3.1 A. Initially purified in DDM. | electron microscopy | J | PC1, 3PE | 5 (best 0.86) |
| 8Q0J | Inward-facing, slack proteoliposome complex I at 3.8 A. Initially purified in DDM. | electron microscopy | J | PC1, 3PE | 4 (best 0.90) |
| 8Q0M | Outward-facing, closed proteoliposome complex I at 3.1 A. Initially purified in DDM. | electron microscopy | J | PC1, CDL, 3PE, PLC | 5 (best 0.86) |
| 8Q0O | Outward-facing, open2 proteoliposome complex I at 3.1 A. Initially purified in DDM. | electron microscopy | J | 3PE, PC1, PLC | 5 (best 0.86) |
| 8Q0Q | Outward-facing, slack proteoliposome complex I at 3.6 A. Initially purified in DDM | electron microscopy | J | PC1, 3PE | 2 (best 0.90) |
| 8Q1P | Inward-facing, open2 proteoliposome complex I at 2.9 A, after deactivation treatment. Initially… | electron microscopy | J | 3PE, PC1 | 4 (best 0.90) |
| 8Q1U | Inward-facing, open1 proteoliposome complex I at 3.3 A, after deactivation treatment. Initially… | electron microscopy | J | 3PE, PC1, CDL | 3 (best 0.86) |
| 8Q1Y | Outward-facing, open2 proteoliposome complex I at 2.6 A, after deactivation treatment. Initially… | electron microscopy | J | PC1, 3PE, PLC | 3 (best 0.86) |
| 8Q25 | Outward-facing, open1 proteoliposome complex I at 2.8 A, after deactivation treatment. Initially… | electron microscopy | J | 3PE, CDL, PC1, PLC | 6 (best 0.87) |
| 8Q45 | Inward-facing, closed proteoliposome complex I at 2.7 A. Initially purified in LMNG. | electron microscopy | J | 3PE, PC1, CDL, PLC | 6 (best 0.86) |
| 8Q46 | Inward-facing, open2 proteoliposome complex I at 2.6 A. Initially purified in LMNG. | electron microscopy | J | PC1, 3PE | 4 (best 0.89) |
| 8Q47 | Inward-facing, open1 proteoliposome complex I at 2.9 A. Initially purified in LMNG. | electron microscopy | J | 3PE, PC1, CDL | 4 (best 0.86) |
| 8Q48 | Outward-facing, closed proteoliposome complex I at 2.5 A. Initially purified in LMNG. | electron microscopy | J | PC1, 3PE, CDL, PLC | 4 (best 0.90) |
| 8Q49 | Outward-facing, open2 proteoliposome complex I at 2.6 A. Initially purified in LMNG. | electron microscopy | J | PC1, 3PE, PLC | 3 (best 0.86) |
| 8Q4A | Outward-facing, open1 proteoliposome complex I at 2.6 A. Initially purified in LMNG. | electron microscopy | J | PC1, 3PE, CDL, PLC | 5 (best 0.87) |
| P03924 | AlphaFold monomer V2.0 prediction for NADH-ubiquinone oxidoreductase chain 6 (P03924) | — | — | — |
Ligands
Elsewhere
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