Research workbench
Crystal structure of galactoside O-acetyltransferase complex with CoA (H3 space group)
Analyse Crystal structure of galactoside O-acetyltransferase complex with CoA (H3 space… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5U2K
- Type
- protein
- Length
- 190 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Galactoside O-acetyltransferase
- EC
- 2.3.1.-
- UniProt
- Q5HCZ5
- Ligands
- COA, CL, PO4
Structure
x-ray diffraction · 1 distinct chain · 22% helix, 30% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Galactoside O-acetyltransferase (EC 2.3.1.-) | protein | 190 | 22% helix, 30% strand | Q5HCZ5 |
Ligands and binding sites
- COA · Coenzyme A · ligand · chains A
- CL · Chloride ion · ion · chains A
- PO4 · Phosphate ion · ion · chains A
- EDO · 1,2-ethanediol · additive · 5 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 5U2K · Crystal structure of Galactoside O-acetyltransferase complex with CoA (H3 space group) · the same entry in another collection · chain A against A, TM-score 1.00
- Q5HCZ5 · AlphaFold monomer V2.0 prediction for putative acetyltransferase SACOL2570 (Q5HCZ5) · a predicted model of the same protein · chain A against A, TM-score 0.98
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 Q5HCZ5
- Elsewhere: RCSB PDB 5U2K · PDBe 5U2K · UniProt Q5HCZ5
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