Research workbench
Crystal structure of fnr of a. fischeri in a partially degraded form
Analyse Crystal structure of fnr of a. fischeri in a partially degraded form in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5CVR
- Type
- protein
- Length
- 206 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Fnr type regulator
- UniProt
- Q70ET4
- Ligands
- FES
- Pockets
- 2 · best druggability 0.66
Structure
x-ray diffraction · 1 distinct chain · 44% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Fnr type regulator | protein | 206 | 44% helix, 25% strand | Q70ET4 |
Ligands and binding sites
- FES · Fe2/s2 (inorganic) cluster · ligand · chains A
- MPD · (4S)-2-methyl-2,4-pentanediol · additive · 3 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 366 | 0.66 | 0.80 | 44 | MPD |
| 2 | 161 | 0.44 | 0.74 | 27 | empty |
Compared structures
- 5CVR · Crystal structure of FNR of A. fischeri in a partially degraded form · 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 Q70ET4
- Elsewhere: RCSB PDB 5CVR · PDBe 5CVR · UniProt Q70ET4
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