Research workbench
Udp-glucose glycoprotein glucosyltransferase from chaetomium thermophilum double mutant D611C:G1050C
Analyse Udp-glucose glycoprotein glucosyltransferase from chaetomium thermophilum… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5NV4
- Type
- protein
- Length
- 1,377 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, BMA
- Pockets
- 20 · best druggability 0.81
Structure
x-ray diffraction · 1 distinct chain · 38% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Udp-glucose-glycoprotein glucosyltransferase-like protein | protein | 1377 | 38% helix, 18% strand | G0SB58 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 6 copies · chains A
- BMA · beta-D-mannopyranose · sugar
- FMT · Formic acid · additive · 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 | 579 | 0.81 | 0.86 | 61 | empty |
| 2 | 933 | 0.80 | 0.82 | 76 | FMT |
| 3 | 320 | 0.72 | 0.85 | 32 | empty |
| 4 | 233 | 0.69 | 0.85 | 30 | empty |
| 5 | 389 | 0.68 | 0.80 | 39 | empty |
Modifications
Observed in the structure: 5 glycan, 4 disulfide (N-glycosylation, disulfide).
Compared structures
- 5NV4 · UDP-Glucose Glycoprotein Glucosyltransferase from Chaetomium thermophilum double mutant… · 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 5NV4 · PDBe 5NV4 · UniProt G0SB58
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