Research workbench
Crystal structure of the actinobacillus pleuropneumoniae HMW1C glycosyltransferase in complex with udp-glc
Analyse Crystal structure of the actinobacillus pleuropneumoniae HMW1C… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3Q3H
- Type
- protein
- Length
- 1,215 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- HMW1C-like glycosyltransferase
- UniProt
- E0EAD4
- Ligands
- UDP
- Pockets
- 6 · best druggability 0.79
Structure
x-ray diffraction · 2 distinct chains · 50% helix, 11% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | HMW1C-like glycosyltransferase | protein | 620 | 49% helix, 11% strand | E0EAD4 |
| B | HMW1C-like glycosyltransferase | protein | 595 | 52% helix, 11% strand | E0EAD4 |
Ligands and binding sites
- UDP · Uridine-5'-diphosphate · ligand · 2 copies · chains A, B
- GOL · Glycerol · additive · 2 copies · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1065 | 0.79 | 0.81 | 99 | UDP |
| 2 | 907 | 0.77 | 0.80 | 87 | UDP, GOL |
| 3 | 133 | 0.46 | 0.77 | 17 | empty |
| 4 | 65 | 0.37 | 0.78 | 16 | empty |
| 5 | 58 | 0.32 | 0.76 | 13 | empty |
Compared structures
- 3Q3H · Crystal structure of the Actinobacillus pleuropneumoniae HMW1C glycosyltransferase in… · 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 E0EAD4
- Elsewhere: RCSB PDB 3Q3H · PDBe 3Q3H · UniProt E0EAD4
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