MolNFT v1 · #47661 · protein
Crystal structure of alpha-2,3-sialyltransferase from campylobacter jejuni in apo form
2P56: “Crystal structure of alpha-2,3-sialyltransferase from campylobacter jejuni in apo form”. X-ray diffraction, 2 pockets (best druggability 0.50). MolNFT v1 #47661 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 2P56
- Type
- protein
- Length
- 257 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Alpha-2,3-sialyltransferase
- EC
- 2.4.99.-
- UniProt
- Q9RGF1
- Pockets
- 2 · best druggability 0.50
Structure
x-ray diffraction · 1 distinct chain · 40% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Alpha-2,3-sialyltransferase (EC 2.4.99.-) | protein | 257 | 40% helix, 14% strand | Q9RGF1 |
Ligands and binding sites
- EDO · 1,2-ethanediol · additive · 5 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 232 | 0.50 | 0.75 | 38 | EDO |
| 2 | 53 | 0.27 | 0.74 | 12 | EDO |
Compared structures
- 2P56 · Crystal structure of alpha-2,3-sialyltransferase from Campylobacter jejuni in apo form · 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 Q9RGF1
- Elsewhere: RCSB PDB 2P56 · PDBe 2P56 · UniProt Q9RGF1
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