Research workbench
Crystal structure of ABBA+UDP+GAL with mpd as the cryoprotectant
Analyse Crystal structure of ABBA+UDP+GAL with mpd 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
- 3SX8
- Type
- protein
- Length
- 274 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 0.48
Structure
x-ray diffraction · 1 distinct chain · 31% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Histo-blood group abo system transferase (EC 2.4.1.37) | protein | 274 | 31% helix, 20% 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
- 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, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 224 | 0.48 | 0.74 | 23 | UDP, GAL |
| 2 | 59 | 0.34 | 0.77 | 18 | empty |
| 3 | 53 | 0.28 | 0.74 | 11 | empty |
Compared structures
- 3SX8 · Crystal structure of ABBA+UDP+Gal with MPD 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 3SX8 · PDBe 3SX8 · UniProt P16442
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