Research workbench
Crystal structure of a. thaliana sugar transport protein 10 in complex with glucose in the outward occluded state
Analyse Crystal structure of a. thaliana sugar transport protein 10 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
- 6H7D
- Type
- protein
- Length
- 487 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q9LT15
- Ligands
- BGC, PO4
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 487 | — | Q9LT15 |
Ligands and binding sites
- BGC · beta-D-glucopyranose · sugar · chains A
- PO4 · Phosphate ion · ion · chains A
- OLC · (2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate · additive · 5 copies · chains A
- P33 · 3,6,9,12,15,18-hexaoxaicosane-1,20-diol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6H7D · Crystal Structure of A. thaliana Sugar Transport Protein 10 in complex with glucose in… · the same entry in another collection · chain A against A, TM-score 1.00
- Q9LT15 · AlphaFold monomer V2.0 prediction for sugar transport protein 10 (Q9LT15) · a predicted model of the same protein · chain A against A, TM-score 0.89
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 Q9LT15
- Elsewhere: RCSB PDB 6H7D · PDBe 6H7D · UniProt Q9LT15
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