Research workbench
Crystal structure of human galactosyltransferase (gtb) complexed with galactose-grease
Analyse Crystal structure of human galactosyltransferase (gtb) complexed with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1ZJP
- Type
- protein
- Length
- 261 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Abo blood group (transferase a, alpha 1-3-N- acetylgalactosaminyltransferase
- UniProt
- P16442
- Ligands
- DR4, UDP, HG, MN, CL
- Pockets
- 2 · best druggability 0.52
Structure
x-ray diffraction · 1 distinct chain · 30% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Abo blood group (transferase a, alpha 1-3-N- acetylgalactosaminyltransferase | protein | 261 | 30% helix, 22% strand | P16442 |
Ligands and binding sites
- DR4 · Methyl 9-(beta-D-talopyranosyloxy)nonanoate · ligand · chains A
- UDP · Uridine-5'-diphosphate · ligand · chains A
- HG · Mercury (II) ion · metal · 6 copies · chains A
- MN · Manganese (II) ion · metal · chains A
- CL · Chloride ion · ion · 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 | 246 | 0.52 | 0.75 | 29 | HG, CL |
| 2 | 57 | 0.29 | 0.74 | 15 | MN |
Compared structures
- 1ZJP · Crystal Structure of Human Galactosyltransferase (GTB) Complexed with Galactose-grease · 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 1ZJP · PDBe 1ZJP · UniProt P16442
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