MolNFT v1 · #161972 · protein
Crystal structure of glutathionylated glycolytic glyceraldehyde-3- phosphate dehydrogenase from arabidopsis thaliana (ATGAPC1)
6QUQ: “Crystal structure of glutathionylated glycolytic glyceraldehyde-3- phosphate dehydrogenase from arabidopsis…”. X-ray diffraction, 3 ligands (NAD, GSH, SO4). MolNFT v1 #161972 on GenesisL1: 3D structure, binding sites and pockets in…
- PDB
- 6QUQ
- Type
- protein
- Length
- 667 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P25858
- Ligands
- NAD, GSH, SO4
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| O | — | protein | 333 | — | P25858 |
| R | — | protein | 334 | — | P25858 |
Ligands and binding sites
- NAD · Nicotinamide-adenine-dinucleotide · ligand · 2 copies · chains O, R
- GSH · Glutathione · ligand · 2 copies · chains O, R
- SO4 · Sulfate ion · ion · 7 copies · chains O, R
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6QUQ · Crystal structure of glutathionylated glycolytic glyceraldehyde-3- phosphate… · the same entry in another collection · chain O against O, TM-score 1.00
- P25858 · AlphaFold monomer V2.0 prediction for glyceraldehyde-3-phosphate dehydrogenase GAPC1… · a predicted model of the same protein · chain O 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 P25858
- Elsewhere: RCSB PDB 6QUQ · PDBe 6QUQ · UniProt P25858
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