Research workbench
Copper-bound E46Q variant of uropathogenic escherichia COLI strain F11 fetp
Analyse Copper-bound E46Q variant of uropathogenic escherichia COLI strain F11 fetp in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5I0Y
- Type
- protein
- Length
- 308 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Periplasmic protein-probably involved in high-affinity FE2+ transport
- UniProt
- A0A0J9WZP9
- Ligands
- CU
- Pockets
- 1 · best druggability 0.39
Structure
x-ray diffraction · 2 distinct chains · 2% helix, 48% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Periplasmic protein-probably involved in high-affinity FE2+ transport | protein | 150 | 2% helix, 51% strand | A0A0J9WZP9 |
| B | Periplasmic protein-probably involved in high-affinity FE2+ transport | protein | 158 | 2% helix, 46% strand | A0A0J9WZP9 |
Ligands and binding sites
- CU · Copper (II) ion · metal · 2 copies · chains A, B
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 | 55 | 0.39 | 0.81 | 15 | empty |
Interfaces
1 interface between chains.
- A–B · 1680 Ų buried · 26 hydrogen bonds · protein-protein
Compared structures
- 5I0Y · Copper-bound E46Q variant of uropathogenic escherichia COLI strain F11 fetp · 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 A0A0J9WZP9
- Elsewhere: RCSB PDB 5I0Y · PDBe 5I0Y · UniProt A0A0J9WZP9
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