Research workbench
Structure of mycobacterium thermoresistibile trehalose-6-phosphate synthase in a complex with trehalose-6-phosphate.
Analyse Structure of mycobacterium thermoresistibile trehalose-6-phosphate synthase in… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5K44
- Type
- protein
- Length
- 460 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- A0A117IMA6
- Ligands
- GLC, G6P
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 460 | — | A0A117IMA6 |
Ligands and binding sites
- GLC · alpha-D-glucopyranose · sugar · chains A
- G6P · 6-O-phosphono-alpha-D-glucopyranose · sugar · chains A
- EDO · 1,2-ethanediol · additive · 3 copies · chains A
- NHE · 2-[N-cyclohexylamino]ethane sulfonic acid · additive · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 5K44 · Structure of Mycobacterium thermoresistibile trehalose-6-phosphate synthase in a complex… · the same entry in another collection · 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 A0A117IMA6
- Elsewhere: RCSB PDB 5K44 · PDBe 5K44 · UniProt A0A117IMA6
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