MolNFT v1 · #152011 · protein
Crystal structure of the disease-causing G426E mutant of the human dihydrolipoamide dehydrogenase
6I4U: “Crystal structure of the disease-causing G426E mutant of the human dihydrolipoamide dehydrogenase”. X-ray diffraction, 2 ligands (FAD, SO4). MolNFT v1 #152011 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6I4U
- Type
- protein
- Length
- 954 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P09622
- Ligands
- FAD, SO4
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 472 | — | P09622 |
| B | — | protein | 482 | — | P09622 |
Ligands and binding sites
- FAD · Flavin-adenine dinucleotide · ligand · 2 copies · chains A, B
- SO4 · Sulfate ion · ion · 9 copies · chains A, B
- 1PE · Pentaethylene glycol · additive · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6I4U · Crystal structure of the disease-causing G426E mutant of the human dihydrolipoamide… · the same entry in another collection · chain A against A, TM-score 1.00
- P09622 · AlphaFold monomer V2.0 prediction for dihydrolipoyl dehydrogenase, mitochondrial (P09622) · a predicted model of the same protein · chain A against A, 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 P09622
- Elsewhere: RCSB PDB 6I4U · PDBe 6I4U · UniProt P09622
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