Research workbench
Crystallographic analysis of the polysialic acid O- acetyltransferase oatwy
Analyse Crystallographic analysis of the polysialic acid O- acetyltransferase oatwy in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2WLC
- Type
- protein
- Length
- 211 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Polysialic acid O-acetyltransferase
- UniProt
- Q93S40
- Ligands
- PO4
Structure
x-ray diffraction · 1 distinct chain · 4% helix, 39% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Polysialic acid O-acetyltransferase | protein | 211 | 4% helix, 39% strand | Q93S40 |
Ligands and binding sites
- PO4 · Phosphate ion · ion · 5 copies · chains A
- EDO · 1,2-ethanediol · additive · 5 copies · chains A
- ACT · Acetate ion · additive · 3 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 2WLC · Crystallographic analysis of the polysialic acid O-acetyltransferase OatWY · the same entry in another collection · chain A against A, TM-score 1.00
- Q93S40 · AlphaFold monomer V2.0 prediction for polysialic acid O-acetyltransferase (Q93S40) · a predicted model of the same protein · chain A 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 Q93S40
- Elsewhere: RCSB PDB 2WLC · PDBe 2WLC · UniProt Q93S40
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