Research workbench
Cryo-EM structure of respiratory complex I from yarrowia lipolytica
Analyse Cryo-EM structure of respiratory complex I from yarrowia lipolytica in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6GCS
- Type
- protein
- Length
- 7,515 residues
- Chains
- 42
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 75-kda protein (nuam); 51-kda protein (nubm); 49-kda protein (nucm); Nimm subunit; Nuem…
- EC
- 1.6.99.3, 1.6.5.3
- UniProt
- Q9UUU3, Q9UUU2, Q9UUU1, A0A1D8NC63, Q6C7X4, Q6C4W9, Q9UUU0, Q9UUT9, Q9UUT8, Q6C674, Q9UUT7, Q9B6D4, A0A1H6Q8Z5, A0A1H6PXT9, A0A1D8N3C8, A0A1D8NG21, A0A1D8NDL1, Q6CGB4, A0A1H6PPE5, A0A1D8NKB4, A0A1D8N7X0, B5FVE5, A0A1D8N596, A0A1H6PJS3, A0A1D8NJR0, Q6CG53, Q6ZY24, Q9B6E8, Q9B6C8, Q9B6C7, Q9B6D6, Q9B6D3, Q9B6E9, A0A1H6PKH9, A0A1D8NNZ0
- Ligands
- SF4, 3PE, FES, FMN, NDP, ZMP, CDL, ZN
- Pockets
- 20 · best druggability 0.90
Structure
electron microscopy · 42 distinct chains · 45% helix, 6% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 75-kda protein (nuam) (EC 1.6.99.3) | protein | 689 | 28% helix, 13% strand | Q9UUU3 |
| B | 51-kda protein (nubm) (EC 1.6.5.3, 1.6.99.3) | protein | 443 | 40% helix, 12% strand | Q9UUU2 |
| C | 49-kda protein (nucm) (EC 1.6.99.3) | protein | 416 | 42% helix, 11% strand | Q9UUU1 |
| D | Nimm subunit | protein | 80 | 51% helix, 6% strand | A0A1D8NC63 |
| E | Nuem subunit | protein | 318 | 30% helix, 11% strand | Q6C7X4 |
| F | Nufm subunit | protein | 119 | 51% helix, 0% strand | Q6C4W9 |
| G | 30-kda protein (nugm) (EC 1.6.99.3) | protein | 232 | 15% helix, 17% strand | Q9UUU0 |
| H | 24-kda subunit (nuhm) (EC 1.6.99.3) | protein | 185 | 37% helix, 10% strand | Q9UUT9 |
| I | Tyky subunit (nuim) (EC 1.6.99.3) | protein | 180 | 26% helix, 12% strand | Q9UUT8 |
| J | Nujm subunit | protein | 140 | 51% helix, 0% strand | Q6C674 |
| K | Psst subunit (nukm) (EC 1.6.99.3) | protein | 169 | 34% helix, 11% strand | Q9UUT7 |
| L | ND4L subunit (nulm) (EC 1.6.5.3) | protein | 86 | 72% helix, 0% strand | Q9B6D4 |
| M | Numm subunit | protein | 105 | 6% helix, 13% strand | A0A1H6Q8Z5 |
| O | ACPM1 subunit | protein | 77 | 51% helix, 3% strand | A0A1H6PXT9 |
| P | NB4M subunit | protein | 116 | 55% helix, 0% strand | A0A1D8N3C8 |
| Q | ACPM2 subunit | protein | 85 | 49% helix, 2% strand | A0A1D8NG21 |
| R | NI2M subunit | protein | 102 | 50% helix, 0% strand | A0A1D8NDL1 |
| S | Nesm subunit (EC 1.6.5.3) | protein | 159 | 55% helix, 0% strand | — |
| U | Nupm subunit | protein | 158 | 53% helix, 2% strand | Q6CGB4 |
| W | NB6M subunit | protein | 118 | 55% helix, 0% strand | A0A1H6PPE5 |
| X | Nuxm subunit | protein | 117 | 39% helix, 0% strand | A0A1D8NKB4 |
| Y | Nuym subunit | protein | 115 | 16% helix, 14% strand | A0A1D8N7X0 |
| Z | Nuzm subunit (EC 1.6.5.3) | protein | 137 | 18% helix, 4% strand | — |
| a | Niam subunit (EC 1.6.5.3) | protein | 100 | 13% helix, 0% strand | — |
| b | Nebm subunit (EC 1.6.5.3) | protein | 64 | 70% helix, 0% strand | — |
| c | NB2M subunit | protein | 42 | 50% helix, 0% strand | B5FVE5 |
| d | Nidm subunit | protein | 89 | 55% helix, 0% strand | A0A1D8N596 |
| e | Nuum subunit (EC 1.6.5.3) | protein | 45 | 47% helix, 0% strand | — |
| f | NI8M subunit | protein | 80 | 26% helix, 25% strand | A0A1H6PJS3 |
| g | NI9M subunit | protein | 60 | 38% helix, 0% strand | A0A1D8NJR0 |
| h | N7BM subunit | protein | 130 | 15% helix, 5% strand | Q6CG53 |
| i | Unknown subunit (EC 1.6.5.3) | protein | 53 | 60% helix, 0% strand | — |
| j | NB5M subunit (EC 1.6.99.3) | protein | 73 | 42% helix, 0% strand | Q6ZY24 |
| n | Nunm subunit (EC 1.6.5.3) | protein | 93 | 42% helix, 0% strand | — |
| 1 | ND1 subunit (NU1M) (EC 1.6.5.3) | protein | 340 | 65% helix, 0% strand | Q9B6E8 |
| 2 | ND2 subunit (NU2M) (EC 1.6.5.3) | protein | 452 | 65% helix, 2% strand | Q9B6C8 |
| 3 | ND3 subunit (NU3M) (EC 1.6.5.3) | protein | 110 | 58% helix, 0% strand | Q9B6C7 |
| 4 | ND4 subunit (NU4M) (EC 1.6.5.3) | protein | 475 | 56% helix, 0% strand | Q9B6D6 |
| 5 | ND5 subunit (NU5M) (EC 1.6.5.3) | protein | 639 | 61% helix, 2% strand | Q9B6D3 |
| 6 | ND6 subunit (NU6M) (EC 1.6.5.3) | protein | 183 | 63% helix, 2% strand | Q9B6E9 |
| 8 | NB8M subunit | protein | 82 | 63% helix, 0% strand | A0A1H6PKH9 |
| 9 | Nipm subunit | protein | 59 | 58% helix, 0% strand | A0A1D8NNZ0 |
Ligands and binding sites
- SF4 · Iron/sulfur cluster · ligand · 6 copies · chains A, C, B, I, K
- 3PE · 1,2-diacyl-sn-glycero-3-phosphoethanolamine · ligand · 3 copies · chains g, 1, 2, 3, C, I, W, b, 4
- FES · Fe2/s2 (inorganic) cluster · ligand · 2 copies · chains A, H
- FMN · Flavin mononucleotide · ligand · chains B
- NDP · Nadph dihydro-nicotinamide-adenine-dinucleotide phosphate · ligand · chains E, K
- ZMP · S-[2-({N-[(2S)-2-hydroxy-3,3-dimethyl-4-(phosphonooxy) butanoyl]-beta-alanyl}amino)ethyl] tetradecanethioate · ligand · chains O, P
- CDL · Cardiolipin · ligand · chains X, g, 2, 3, 6
- ZN · Zinc ion · metal · chains M
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1084 | 0.90 | 0.92 | 127 | NDP |
| 2 | 1116 | 0.89 | 0.91 | 107 | empty |
| 3 | 1117 | 0.88 | 0.90 | 117 | empty |
| 4 | 924 | 0.88 | 0.90 | 132 | empty |
| 5 | 875 | 0.88 | 0.90 | 146 | empty |
Interfaces
174 interfaces between chains.
- 1–3 · 2735 Ų buried · 6 hydrogen bonds · protein-protein
- C–G · 2681 Ų buried · 19 hydrogen bonds · protein-protein
- A–Y · 2484 Ų buried · 26 hydrogen bonds · protein-protein
- L–6 · 2428 Ų buried · 4 hydrogen bonds · protein-protein
- B–H · 2377 Ų buried · 18 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 8 disulfide, 1 covalent (disulfide, covalent ligand).
Compared structures
- 6GCS · Cryo-EM structure of respiratory complex I from Yarrowia lipolytica · the same entry in another collection · chain K against K, TM-score 1.00
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt Q9UUU3
- Every structure of UniProt Q9UUU2
- Every structure of UniProt Q9UUU1
- Every structure of UniProt A0A1D8NC63
- Every structure of UniProt Q6C7X4
- Every structure of UniProt Q6C4W9
- Every structure of UniProt Q9UUU0
- Every structure of UniProt Q9UUT9
- Every structure of UniProt Q9UUT8
- Every structure of UniProt Q6C674
- Every structure of UniProt Q9UUT7
- Every structure of UniProt Q9B6D4
- Every structure of UniProt A0A1H6Q8Z5
- Every structure of UniProt A0A1H6PXT9
- Every structure of UniProt A0A1D8N3C8
- Every structure of UniProt A0A1D8NG21
- Every structure of UniProt A0A1D8NDL1
- Every structure of UniProt Q6CGB4
- Every structure of UniProt A0A1H6PPE5
- Every structure of UniProt A0A1D8NKB4
- Every structure of UniProt A0A1D8N7X0
- Every structure of UniProt B5FVE5
- Every structure of UniProt A0A1D8N596
- Every structure of UniProt A0A1H6PJS3
- Every structure of UniProt A0A1D8NJR0
- Every structure of UniProt Q6CG53
- Every structure of UniProt Q6ZY24
- Every structure of UniProt Q9B6E8
- Every structure of UniProt Q9B6C8
- Every structure of UniProt Q9B6C7
- Every structure of UniProt Q9B6D6
- Every structure of UniProt Q9B6D3
- Every structure of UniProt Q9B6E9
- Every structure of UniProt A0A1H6PKH9
- Every structure of UniProt A0A1D8NNZ0
- Elsewhere: RCSB PDB 6GCS · PDBe 6GCS · UniProt Q9UUU3 · UniProt Q9UUU2 · UniProt Q9UUU1 · UniProt A0A1D8NC63 · UniProt Q6C7X4 · UniProt Q6C4W9 · UniProt Q9UUU0 · UniProt Q9UUT9 · UniProt Q9UUT8 · UniProt Q6C674 · UniProt Q9UUT7 · UniProt Q9B6D4 · UniProt A0A1H6Q8Z5 · UniProt A0A1H6PXT9 · UniProt A0A1D8N3C8 · UniProt A0A1D8NG21 · UniProt A0A1D8NDL1 · UniProt Q6CGB4 · UniProt A0A1H6PPE5 · UniProt A0A1D8NKB4 · UniProt A0A1D8N7X0 · UniProt B5FVE5 · UniProt A0A1D8N596 · UniProt A0A1H6PJS3 · UniProt A0A1D8NJR0 · UniProt Q6CG53 · UniProt Q6ZY24 · UniProt Q9B6E8 · UniProt Q9B6C8 · UniProt Q9B6C7 · UniProt Q9B6D6 · UniProt Q9B6D3 · UniProt Q9B6E9 · UniProt A0A1H6PKH9 · UniProt A0A1D8NNZ0
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