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Crystallographic structure of the native bovine alpha-1,3- galactosyltransferase catalytic domain
Analyse Crystallographic structure of the native bovine alpha-1,3… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1G8O
- Type
- protein
- Length
- 287 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- N-acetyllactosaminide alpha-1,3-galactosyltransferase
- EC
- 2.4.1.151
- UniProt
- P14769
- Ligands
- U5P, MN
- Pockets
- 3 · best druggability 0.77
Structure
x-ray diffraction · 1 distinct chain · 36% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | N-acetyllactosaminide alpha-1,3-galactosyltransferase (EC 2.4.1.151) | protein | 287 | 36% helix, 21% strand | P14769 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 148 | 0.77 | 0.94 | 24 | U5P |
| 2 | 104 | 0.40 | 0.76 | 19 | empty |
| 3 | 61 | 0.39 | 0.80 | 16 | empty |
Compared structures
- 1G8O · Crystallographic structure of the native bovine alpha-1,3-galactosyltransferase catalytic… · the same entry in another collection · chain A against A, TM-score 1.00
- P14769 · AlphaFold monomer V2.0 prediction for N-acetyllactosaminide… · a predicted model of the same protein · chain A against A, TM-score 0.97
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 P14769
- Elsewhere: RCSB PDB 1G8O · PDBe 1G8O · UniProt P14769
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