Research workbench
Natural occuring mutation of human ABO(H) galactosyltransferase: GTB/M214R
Analyse Natural occuring mutation of human ABO(H) galactosyltransferase: GTB/M214R in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2O1F
- Type
- protein
- Length
- 264 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Abo glycosyltransferase
- UniProt
- Q70V27
- Ligands
- HG
- Pockets
- 2 · best druggability 0.56
Structure
x-ray diffraction · 1 distinct chain · 30% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Abo glycosyltransferase | protein | 264 | 30% helix, 22% strand | Q70V27 |
Ligands and binding sites
- HG · Mercury (II) ion · metal · 3 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 | 301 | 0.56 | 0.76 | 35 | HG |
| 2 | 68 | 0.31 | 0.74 | 12 | empty |
Compared structures
- 2O1F · Natural Occuring Mutation of Human ABO(H) galactosyltransferase: GTB/M214R · the same entry in another collection · 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 Q70V27
- Elsewhere: RCSB PDB 2O1F · PDBe 2O1F · UniProt Q70V27
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