MolNFT v1 · #29723 · protein
Crystal structure of human N-acetylgalactosaminyltransferase (gta) complexed with galactose
1ZHJ · Histo-blood group abo system transferase (nagat) includes…: “Crystal structure of human N-acetylgalactosaminyltransferase (gta) complexed with galactose”. X-ray diffraction, 3 ligands (GAL, HG, CL), 2 pockets (best druggability…
- PDB
- 1ZHJ
- Type
- protein
- Length
- 272 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Histo-blood group abo system transferase (nagat) includes…
- EC
- 2.4.1.40
- UniProt
- P16442
- Ligands
- GAL, HG, CL
- Pockets
- 2 · best druggability 0.59
Structure
x-ray diffraction · 1 distinct chain · 29% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Histo-blood group abo system transferase (nagat) includes: glycoprotein-fucosylgalactoside alpha-N- acetylgalactosaminyltransferase (EC 2.4.1.40) | protein | 272 | 29% helix, 21% strand | P16442 |
Ligands and binding sites
- GAL · beta-D-galactopyranose · sugar · chains A
- HG · Mercury (II) ion · metal · 5 copies · chains A
- CL · Chloride ion · ion · 2 copies · 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 | 338 | 0.59 | 0.76 | 34 | HG, CL |
| 2 | 50 | 0.24 | 0.72 | 13 | empty |
Compared structures
- 1ZHJ · Crystal Structure of human N-acetylgalactosaminyltransferase (GTA) Complexed with… · 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 0.98
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 1ZHJ · PDBe 1ZHJ · UniProt P16442
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