Research workbench
Human mcu-emre complex
Analyse Human mcu-emre complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6K7X
- Type
- protein
- Length
- 2,622 residues
- Chains
- 16
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q8NE86, Q9H4I9
- Ligands
- PLX, CDL, CA
Structure
electron microscopy · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| C, K | — | protein | 276 | — | Q8NE86 |
| A, B, D, L, M, N | — | protein | 273 | — | Q8NE86 |
| H, E, F, G, O, P, Q, R | — | protein | 54 | — | Q9H4I9 |
Ligands and binding sites
- PLX · (9R,11S)-9-({[(1S)-1-hydroxyhexadecyl]oxy}methyl)-2,2-dimethyl-5,7,10-trioxa-2lambda~5~-aza-6lambda~5~-phosphaoctacosane-6,6,11-triol · ligand · 16 copies · chains C, A, G, B, D, K, L, R, M, N
- CDL · Cardiolipin · ligand · 8 copies · chains C, D, E, A, F, B, G, H, K, N, P, L, Q, M, R, O
- CA · Calcium ion · metal · 6 copies · chains C, A, B, D, K, L, M, N
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6K7X · Human MCU-EMRE complex · the same entry in another collection · chain M against M, 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 Q8NE86
- Every structure of UniProt Q9H4I9
- Elsewhere: RCSB PDB 6K7X · PDBe 6K7X · UniProt Q8NE86 · UniProt Q9H4I9
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