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
- 2WLD
- Type
- protein
- Length
- 632 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Polysialic acid O-acetyltransferase
- UniProt
- Q93S40
- Pockets
- 3 · best druggability 0.79
Structure
x-ray diffraction · 2 distinct chains · 5% helix, 44% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Polysialic acid O-acetyltransferase | protein | 210 | 4% helix, 43% strand | Q93S40 |
| B, C | Polysialic acid O-acetyltransferase | protein | 211 | 5% helix, 46% strand | Q93S40 |
Ligands and binding sites
- EDO · 1,2-ethanediol · additive · 7 copies · chains A, B, C
- ACT · Acetate ion · additive · 2 copies · chains A, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 893 | 0.79 | 0.81 | 104 | EDO |
| 2 | 372 | 0.68 | 0.81 | 49 | EDO |
| 3 | 372 | 0.63 | 0.78 | 39 | ACT |
Interfaces
3 interfaces between chains.
- B–C · 1057 Ų buried · 13 hydrogen bonds · protein-protein
- A–C · 1055 Ų buried · 11 hydrogen bonds · protein-protein
- A–B · 1036 Ų buried · 14 hydrogen bonds · protein-protein
Compared structures
- 2WLD · 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 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 Q93S40
- Elsewhere: RCSB PDB 2WLD · PDBe 2WLD · UniProt Q93S40
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