Research workbench
Crystal structure of ABBB+UDP+GAL with glycerol as the cryoprotectant
Analyse Crystal structure of ABBB+UDP+GAL with glycerol as the cryoprotectant in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3SXA
- Type
- protein
- Length
- 291 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Histo-blood group abo system transferase
- EC
- 2.4.1.37
- UniProt
- P16442
- Ligands
- UDP, GAL, MN
- Pockets
- 3 · best druggability 0.73
Structure
x-ray diffraction · 1 distinct chain · 33% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Histo-blood group abo system transferase (EC 2.4.1.37) | protein | 291 | 33% helix, 19% strand | P16442 |
Ligands and binding sites
- UDP · Uridine-5'-diphosphate · ligand · chains A
- GAL · beta-D-galactopyranose · sugar · chains A
- MN · Manganese (II) ion · metal · chains A
- GOL · Glycerol · additive · chains A
- PEG · Di(hydroxyethyl)ether · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 403 | 0.73 | 0.84 | 44 | UDP, GAL, GOL, MN |
| 2 | 56 | 0.43 | 0.83 | 14 | empty |
| 3 | 80 | 0.33 | 0.74 | 15 | empty |
Compared structures
- 3SXA · Crystal structure of ABBB+UDP+Gal with Glycerol as the cryoprotectant · the same entry in another collection · chain A against A, TM-score 1.00
- P16442 · AlphaFold monomer V2.0 prediction for histo-blood group abo system transferase (P16442) · 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 P16442
- Elsewhere: RCSB PDB 3SXA · PDBe 3SXA · UniProt P16442
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