MolNFT v1 · #53810 · protein
Crystal structure of the sialyltransferase cst-II N51A in complex with cmp
2X63 · Alpha-2,3-/2,8-sialyltransferase: “Crystal structure of the sialyltransferase cst-II N51A in complex with cmp”. X-ray diffraction, 1 ligand (C), 1 pocket (best druggability 0.75). MolNFT v1 #53810 on GenesisL1: 3D structure, binding…
- PDB
- 2X63
- Type
- protein
- Length
- 258 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Alpha-2,3-/2,8-sialyltransferase
- EC
- 2.4.99.-
- UniProt
- Q9LAK3
- Ligands
- C
- Pockets
- 1 · best druggability 0.75
Structure
x-ray diffraction · 1 distinct chain · 39% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Alpha-2,3-/2,8-sialyltransferase (EC 2.4.99.-) | protein | 258 | 39% helix, 15% strand | Q9LAK3 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 411 | 0.75 | 0.85 | 45 | C |
Compared structures
- 2X63 · Crystal structure of the sialyltransferase CST-II N51A in complex with CMP · 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 Q9LAK3
- Elsewhere: RCSB PDB 2X63 · PDBe 2X63 · UniProt Q9LAK3
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