Research workbench
Mutant human ABO(H) blood group glycosyltransferase with bound udp and acceptor
Analyse Mutant human ABO(H) blood group glycosyltransferase with bound udp and acceptor in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1WT3
- 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
- EC
- 2.4.1.40
- UniProt
- P16442
- Ligands
- BHG, UDP, FUC, HG
- Pockets
- 1 · best druggability 0.56
Structure
x-ray diffraction · 1 distinct chain · 31% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Histo-blood group abo system transferase (EC 2.4.1.40) | protein | 263 | 31% helix, 22% strand | P16442 |
Ligands and binding sites
- BHG · hexyl beta-D-galactopyranoside · ligand · chains A
- UDP · Uridine-5'-diphosphate · ligand · chains A
- FUC · alpha-L-fucopyranose · sugar · chains A
- HG · Mercury (II) ion · metal · 4 copies · 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 | 288 | 0.56 | 0.76 | 31 | HG, UDP |
Compared structures
- 1WT3 · Mutant human ABO(H) blood group glycosyltransferase with bound UDP and acceptor · 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 1WT3 · PDBe 1WT3 · UniProt P16442
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