MolNFT v1 · #149180 · protein
Catalytic domain of udp-glucose glycoprotein glucosyltransferase from chaetomium thermophilum in complex with udp-glucose (conformation 1)
6FSN · Udp-glucose-glycoprotein glucosyltransferase-like protein: “Catalytic domain of udp-glucose glycoprotein glucosyltransferase from chaetomium thermophilum in complex with…”. X-ray diffraction, 3 ligands (UPG, NAG, CA), 2 pockets…
- PDB
- 6FSN
- Type
- protein
- Length
- 276 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
- UPG, NAG, CA
- Pockets
- 2 · best druggability 0.65
Structure
x-ray diffraction · 1 distinct chain · 45% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Udp-glucose-glycoprotein glucosyltransferase-like protein | protein | 276 | 45% helix, 16% strand | G0SB58 |
Ligands and binding sites
- UPG · Uridine-5'-diphosphate-glucose · ligand · chains A
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · chains A
- CA · Calcium ion · metal · chains A
- EDO · 1,2-ethanediol · additive · chains A
- PGE · Triethylene glycol · additive · 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 | 349 | 0.65 | 0.80 | 29 | CA, UPG |
| 2 | 97 | 0.37 | 0.75 | 14 | empty |
Modifications
Observed in the structure: 2 disulfide, 1 glycan (disulfide, N-glycosylation).
Compared structures
- 6FSN · Catalytic domain of UDP-Glucose Glycoprotein Glucosyltransferase from Chaetomium… · 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 6FSN · PDBe 6FSN · UniProt G0SB58
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