Research workbench
E. COLI glmu- complex with udp-glcnac and acetyl-CoA
Analyse E. COLI glmu- complex with udp-glcnac and acetyl-CoA in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2OI5
- Type
- protein
- Length
- 899 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
- ACO, UD1, MG, SO4
- Pockets
- 5 · best druggability 0.75
Structure
x-ray diffraction · 2 distinct chains · 21% helix, 34% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Bifunctional protein glmu (EC 2.7.7.23, 2.3.1.157) | protein | 449 | 22% helix, 34% strand | P0ACC7 |
| B | Bifunctional protein glmu (EC 2.7.7.23, 2.3.1.157) | protein | 450 | 20% helix, 34% strand | P0ACC7 |
Ligands and binding sites
- ACO · Acetyl coenzyme *A · ligand · 2 copies · chains A, B
- UD1 · Uridine-diphosphate-N-acetylglucosamine · ligand · 2 copies · chains A, B
- MG · Magnesium ion · metal · 5 copies · chains A, B
- SO4 · Sulfate ion · ion · 3 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 442 | 0.75 | 0.84 | 37 | MG, SO4, UD1 |
| 2 | 591 | 0.70 | 0.78 | 57 | UD1 |
| 3 | 128 | 0.42 | 0.76 | 24 | empty |
| 4 | 109 | 0.35 | 0.73 | 17 | empty |
| 5 | 63 | 0.34 | 0.77 | 14 | empty |
Interfaces
1 interface between chains.
- A–B · 141 Ų buried · 1 hydrogen bond · 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 2OI5 · PDBe 2OI5 · UniProt P0ACC7
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