Research workbench
B-specific alpha-1,3-galactosyltransferase \ G176R +UDP+ADA
Analyse B-specific alpha-1,3-galactosyltransferase \ G176R +UDP+ADA in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2RJ4
- Type
- protein
- Length
- 290 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glycoprotein-fucosylgalactoside alpha- galactosyltransferase
- EC
- 2.4.1.37
- UniProt
- P16442
- Ligands
- UDP, AD7, MN
- Pockets
- 3 · best druggability 0.74
Structure
x-ray diffraction · 1 distinct chain · 32% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glycoprotein-fucosylgalactoside alpha- galactosyltransferase (EC 2.4.1.37) | protein | 290 | 32% helix, 19% strand | P16442 |
Ligands and binding sites
- UDP · Uridine-5'-diphosphate · ligand · chains A
- AD7 · octyl 3-amino-3-deoxy-2-O-(2,6-dideoxy-alpha-L-lyxo-hexopyranosyl)-beta-D-galactopyranoside · ligand · chains A
- MN · Manganese (II) ion · metal · 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 | 409 | 0.74 | 0.84 | 40 | MN, UDP, AD7 |
| 2 | 54 | 0.44 | 0.83 | 13 | empty |
| 3 | 58 | 0.29 | 0.74 | 11 | empty |
Compared structures
- 2RJ4 · B-specific alpha-1,3-galactosyltransferase G176R +UDP+ADA · 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 0.99
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 2RJ4 · PDBe 2RJ4 · UniProt P16442
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