Research workbench
Unliganded structure of the human wild type beta-galactoside alpha-2, 6-sialyltransferase 1 (ST6GAL1)
Analyse Unliganded structure of the human wild type beta-galactoside alpha-2… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6QVS
- Type
- protein
- Length
- 539 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Beta-galactoside alpha-2,6-sialyltransferase 1
- EC
- 2.4.99.1
- UniProt
- P15907
- Pockets
- 1 · best druggability 0.79
Structure
x-ray diffraction · 2 distinct chains · 39% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Beta-galactoside alpha-2,6-sialyltransferase 1 (EC 2.4.99.1) | protein | 269 | 39% helix, 14% strand | P15907 |
| B | Beta-galactoside alpha-2,6-sialyltransferase 1 (EC 2.4.99.1) | protein | 270 | 39% helix, 14% strand | P15907 |
Ligands and binding sites
- PEG · Di(hydroxyethyl)ether · additive · 2 copies · chains A, B
- GOL · Glycerol · additive · chains A, B
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 | 847 | 0.79 | 0.82 | 101 | PEG, GOL |
Interfaces
1 interface between chains.
- A–B · 771 Ų buried · 9 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 6 disulfide (disulfide).
Compared structures
- 6QVS · Unliganded structure of the human wild type Beta-galactoside alpha-2,6-sialyltransferase… · the same entry in another collection · chain A against A, TM-score 1.00
- P15907 · AlphaFold monomer V2.0 prediction for beta-galactoside alpha-2,6-sialyltransferase 1… · a predicted model of the same protein · chain B against A, TM-score 0.97
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 P15907
- Elsewhere: RCSB PDB 6QVS · PDBe 6QVS · UniProt P15907
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