Research workbench
M. luteus B-P 26 heterodimeric hexaprenyl diphosphate synthase in complex with magnesium and fpp analogue
Analyse M. luteus B-P 26 heterodimeric hexaprenyl diphosphate synthase in complex with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3AQC
- Type
- protein
- Length
- 916 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- O66127, O66129
Structure
x-ray diffraction · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | — | protein | 135 | — | O66127 |
| B | — | protein | 321 | — | O66129 |
| D | — | protein | 325 | — | O66129 |
Compared structures
- 3AQC · M. luteus B-P 26 heterodimeric hexaprenyl diphosphate synthase in complex with magnesium… · the same entry in another collection · chain A against A, TM-score 1.00
- O66129 · AlphaFold monomer V2.0 prediction for hexaprenyl-diphosphate synthase large subunit… · a predicted model of the same protein · chain B against A, TM-score 0.98
- O66127 · AlphaFold monomer V2.0 prediction for hexaprenyl-diphosphate synthase small subunit… · a predicted model of the same protein · chain A against A, TM-score 0.97
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 O66127
- Every structure of UniProt O66129
- Elsewhere: RCSB PDB 3AQC · PDBe 3AQC · UniProt O66127 · UniProt O66129
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