Research workbench
Crystal structure of fructuronate reductase (ydfi) from E. COLI CFT073 (efi target efi-506389) complexed with NADH and D-mannonate
Analyse Crystal structure of fructuronate reductase (ydfi) from E. COLI CFT073 (efi… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4IM7
- Type
- protein
- Length
- 483 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Hypothetical oxidoreductase ydfi
- EC
- 1.-.-.-
- UniProt
- Q8FHD0
- Ligands
- CS2, NAI, SO4
- Pockets
- 3 · best druggability 0.76
Structure
x-ray diffraction · 1 distinct chain · 52% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Hypothetical oxidoreductase ydfi (EC 1.-.-.-) | protein | 483 | 52% helix, 13% strand | Q8FHD0 |
Ligands and binding sites
- CS2 · D-mannonic acid · ligand · chains A
- NAI · 1,4-dihydronicotinamide adenine dinucleotide · ligand · chains A
- SO4 · Sulfate ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 557 | 0.76 | 0.83 | 55 | CS2, NAI |
| 2 | 128 | 0.46 | 0.78 | 27 | empty |
| 3 | 52 | 0.36 | 0.80 | 14 | empty |
Compared structures
- 4IM7 · Crystal structure of fructuronate reductase (ydfI) from E. coli CFT073 (EFI TARGET… · 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 Q8FHD0
- Elsewhere: RCSB PDB 4IM7 · PDBe 4IM7 · UniProt Q8FHD0
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