Research workbench
E. COLI CFT073 C3406 in complex with A5P
Analyse E. COLI CFT073 C3406 in complex with A5P in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5UQI
- Type
- protein
- Length
- 188 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Phosphosugar isomerase
- UniProt
- A0A0H2VCL5
- Ligands
- A5P
- Pockets
- 1 · best druggability 0.34
Structure
x-ray diffraction · 1 distinct chain · 54% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Phosphosugar isomerase | protein | 188 | 54% helix, 13% strand | A0A0H2VCL5 |
Ligands and binding sites
- A5P · Arabinose-5-phosphate · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 50 | 0.34 | 0.78 | 16 | A5P |
Compared structures
- 5UQI · E. coli CFT073 c3406 in complex with A5P · 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 A0A0H2VCL5
- Elsewhere: RCSB PDB 5UQI · PDBe 5UQI · UniProt A0A0H2VCL5
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