Research workbench
GLMUC1 in complex with an antibacterial inhibitor
Analyse GLMUC1 in complex with an antibacterial inhibitor in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3TWD
- Type
- protein
- Length
- 444 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Bifunctional protein glmu
- EC
- 2.7.7.23, 2.3.1.157
- UniProt
- P0ACC7
- Ligands
- GOB, SO4
- Pockets
- 2 · best druggability 0.72
Structure
x-ray diffraction · 1 distinct chain · 9% helix, 42% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Bifunctional protein glmu (EC 2.7.7.23, 2.3.1.157) | protein | 222 | 9% helix, 42% strand | P0ACC7 |
Ligands and binding sites
- GOB · 4-({5-[(4-aminophenyl)(phenyl)sulfamoyl]-2,4-dimethoxyphenyl}amino)-4-oxobutanoic acid · ligand · 2 copies · chains A, B
- SO4 · Sulfate ion · ion · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 844 | 0.72 | 0.77 | 82 | empty |
| 2 | 239 | 0.69 | 0.86 | 35 | empty |
Interfaces
1 interface between chains.
- A–B · 849 Ų buried · 11 hydrogen bonds · protein-protein
Compared structures
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 P0ACC7
- Elsewhere: RCSB PDB 3TWD · PDBe 3TWD · UniProt P0ACC7
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