Research workbench
Crystal structure of the alpha bata heterodimer of human IDH3 in complex with NADH
Analyse Crystal structure of the alpha bata heterodimer of human IDH3 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
- 6KE3
- Type
- protein
- Length
- 2,650 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P50213, O43837
- Ligands
- NAI
Structure
x-ray diffraction · 5 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 335 | — | P50213 |
| B, D, F, H | — | protein | 338 | — | O43837 |
| C | — | protein | 325 | — | P50213 |
| E | — | protein | 318 | — | P50213 |
| G | — | protein | 320 | — | P50213 |
Ligands and binding sites
- NAI · 1,4-dihydronicotinamide adenine dinucleotide · ligand · 4 copies · chains A, B, C, D, E, F, G, H
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6KE3 · Crystal structure of the alpha bata heterodimer of human IDH3 in complex with NADH · the same entry in another collection · chain H against H, TM-score 1.00
- P50213 · AlphaFold monomer V2.0 prediction for isocitrate dehydrogenase [NAD] subunit alpha… · 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 P50213
- Every structure of UniProt O43837
- Elsewhere: RCSB PDB 6KE3 · PDBe 6KE3 · UniProt P50213 · UniProt O43837
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