MolNFT v1 · #170656 · protein
Arabidopsis thaliana glutamate dehydrogenase isoform 1 in apo form
6YEH: “Arabidopsis thaliana glutamate dehydrogenase isoform 1 in apo form”. X-ray diffraction, 1 ligand (K). MolNFT v1 #170656 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6YEH
- Type
- protein
- Length
- 2,455 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q43314
- Ligands
- K
Structure
x-ray diffraction · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, D, E | — | protein | 410 | — | Q43314 |
| B | — | protein | 409 | — | Q43314 |
| C, F | — | protein | 408 | — | Q43314 |
Ligands and binding sites
- K · Potassium ion · metal · 6 copies · chains A, B, C, D, E, F
- MPD · (4S)-2-methyl-2,4-pentanediol · additive · 11 copies · chains A, E, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6YEH · Arabidopsis thaliana glutamate dehydrogenase isoform 1 in apo form · the same entry in another collection · chain F against F, TM-score 1.00
- Q43314 · AlphaFold monomer V2.0 prediction for glutamate dehydrogenase 1 (Q43314) · a predicted model of the same protein · chain C against A, TM-score 0.99
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 Q43314
- Elsewhere: RCSB PDB 6YEH · PDBe 6YEH · UniProt Q43314
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