MolNFT v1 · #50472 · protein
B-specific alpha-1,3-galactosyltransferase G176R S235G mutant (aabb) + udpgal + deoxy-acceptor
2RJ7 · Glycoprotein-fucosylgalactoside alpha- galactosyltransferase: “B-specific alpha-1,3-galactosyltransferase G176R S235G mutant (aabb) + udpgal + deoxy-acceptor”. X-ray diffraction, 3 ligands (GDU, DA8, MN), 2 pockets (best…
- PDB
- 2RJ7
- Type
- protein
- Length
- 292 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
- GDU, DA8, MN
- Pockets
- 2 · best druggability 0.75
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 | 292 | 32% helix, 19% strand | P16442 |
Ligands and binding sites
- GDU · Galactose-uridine-5'-diphosphate · ligand · chains A
- DA8 · octyl 3-deoxy-2-O-(6-deoxy-alpha-L-galactopyranosyl)-beta-D-xylo-hexopyranoside · 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
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 442 | 0.75 | 0.84 | 45 | GDU, MN, DA8 |
| 2 | 71 | 0.47 | 0.83 | 14 | empty |
Compared structures
- 2RJ7 · B-specific alpha-1,3-galactosyltransferase G176R S235G mutant (AABB) + UDPGal +… · 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 2RJ7 · PDBe 2RJ7 · UniProt P16442
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