Research workbench
The crystal structure of fhue from E. COLI in complex with its substrate coprogen
Analyse The crystal structure of fhue from E. COLI in complex with its substrate… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6E4V
- Type
- protein
- Length
- 672 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Fhue receptor
- UniProt
- P16869
- Ligands
- HWS
- Pockets
- 7 · best druggability 0.88
Structure
x-ray diffraction · 1 distinct chain · 5% helix, 61% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Fhue receptor | protein | 672 | 5% helix, 61% strand | P16869 |
Ligands and binding sites
- HWS · Coprogen · ligand · chains A
- BOG · octyl beta-D-glucopyranoside · additive · 5 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 701 | 0.88 | 0.92 | 85 | empty |
| 2 | 89 | 0.76 | 0.98 | 32 | empty |
| 3 | 487 | 0.74 | 0.83 | 57 | empty |
| 4 | 439 | 0.66 | 0.79 | 56 | HWS |
| 5 | 416 | 0.65 | 0.78 | 36 | empty |
Compared structures
- 6E4V · The Crystal Structure of FhuE from E. coli in complex with its substrate Coprogen · the same entry in another collection · chain A against A, TM-score 1.00
- P16869 · AlphaFold monomer V2.0 prediction for fhue receptor (P16869) · a predicted model of the same protein · 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 P16869
- Elsewhere: RCSB PDB 6E4V · PDBe 6E4V · UniProt P16869
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