Research workbench
Transaldolase variant T30A from T. acidophilum in complex with D- fructose 6-phosphate schiff-base intermediate
Analyse Transaldolase variant T30A from T. acidophilum in complex with D- fructose… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6YRM
- Type
- protein
- Length
- 1,115 residues
- Chains
- 5
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q9HKI3
- Ligands
- F6R
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E | — | protein | 223 | — | Q9HKI3 |
Ligands and binding sites
- F6R · Fructose -6-phosphate · ligand · 5 copies · chains A, B, C, D, E
- GOL · Glycerol · additive · 7 copies · chains A, B, C, D, E
- ACT · Acetate ion · additive · 4 copies · chains A, E, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6YRM · Transaldolase variant T30A from T. acidophilum in complex with D-fructose 6-phosphate… · the same entry in another collection · chain A against A, TM-score 1.00
- Q9HKI3 · AlphaFold monomer V2.0 prediction for probable transaldolase (Q9HKI3) · 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 Q9HKI3
- Elsewhere: RCSB PDB 6YRM · PDBe 6YRM · UniProt Q9HKI3
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