Research workbench
Crystal structure of human N-acetylgalactosaminyltransferase (gta) complexed with beta-methyllactoside
Analyse Crystal structure of human N-acetylgalactosaminyltransferase (gta) complexed… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2A8W
- Type
- protein
- Length
- 263 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Histo-blood group abo system transferase (nagat) [includes…
- UniProt
- P16442
- Ligands
- UDP, HG, MN, CL
- Pockets
- 1 · best druggability 0.53
Structure
x-ray diffraction · 1 distinct chain · 30% helix, 22% 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) (fucosylglycoprotein alpha-N-acetylgalactosaminyltransferase) (histo-blood group a transferase) (a transferase) | protein | 263 | 30% helix, 22% strand | P16442 |
Ligands and binding sites
- UDP · Uridine-5'-diphosphate · ligand · chains A
- HG · Mercury (II) ion · metal · 5 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
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 252 | 0.53 | 0.76 | 29 | HG, CL, UDP |
Compared structures
- 2A8W · 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 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 2A8W · PDBe 2A8W · UniProt P16442
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