Research workbench
Chaetomium thermophilum udp-glucose glucosyl transferase (uggt) purified from cells treated with kifunensine.
Analyse Chaetomium thermophilum udp-glucose glucosyl transferase (uggt) purified from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6TRF
- Type
- protein
- Length
- 1,319 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Udp-glucose-glycoprotein glucosyltransferase-like protein
- UniProt
- G0SB58
- Ligands
- NAG, MAN, BMA, CA
- Pockets
- 20 · best druggability 0.78
Structure
x-ray diffraction · 1 distinct chain · 38% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Udp-glucose-glycoprotein glucosyltransferase-like protein | protein | 1319 | 38% helix, 17% strand | G0SB58 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 4 copies · chains A
- MAN · alpha-D-mannopyranose · sugar · 3 copies · chains A
- BMA · beta-D-mannopyranose · sugar
- CA · Calcium ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 940 | 0.78 | 0.81 | 73 | empty |
| 2 | 509 | 0.74 | 0.82 | 47 | empty |
| 3 | 815 | 0.71 | 0.76 | 56 | empty |
| 4 | 407 | 0.69 | 0.81 | 37 | empty |
| 5 | 529 | 0.69 | 0.79 | 59 | empty |
Modifications
Observed in the structure: 3 disulfide, 2 glycan (disulfide, N-glycosylation).
Compared structures
- 6TRF · Chaetomium thermophilum UDP-Glucose Glucosyl Transferase (UGGT) purified from cells… · 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 G0SB58
- Elsewhere: RCSB PDB 6TRF · PDBe 6TRF · UniProt G0SB58
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