Research workbench
Cryo-EM structure of human mitochondrial translocase tom complex at 3.0 ångström.
Analyse Cryo-EM structure of human mitochondrial translocase tom complex at 3.0… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7CP9
- Type
- protein
- Length
- 1,021 residues
- Chains
- 10
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q8N4H5, Q96B49, Q9P0U1, Q9NS69, O96008
- Ligands
- PC1
Structure
electron microscopy · 6 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 38 | — | Q8N4H5 |
| B | — | protein | 37 | — | Q8N4H5 |
| C, D | — | protein | 49 | — | Q96B49 |
| E, F | — | protein | 52 | — | Q9P0U1 |
| G, H | — | protein | 86 | — | Q9NS69 |
| I, J | — | protein | 286 | — | O96008 |
Ligands and binding sites
- PC1 · 1,2-diacyl-sn-glycero-3-phosphocholine · ligand · 11 copies · chains C, I, E, J, F, G, H, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
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 Q8N4H5
- Every structure of UniProt Q96B49
- Every structure of UniProt Q9P0U1
- Every structure of UniProt Q9NS69
- Every structure of UniProt O96008
- Elsewhere: RCSB PDB 7CP9 · PDBe 7CP9 · UniProt Q8N4H5 · UniProt Q96B49 · UniProt Q9P0U1 · UniProt Q9NS69 · UniProt O96008
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