Research workbench
Crystal structure of E. COLI wrba in complex with FMN
Analyse Crystal structure of E. COLI wrba in complex with FMN in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2R96
- Type
- protein
- Length
- 394 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Flavoprotein wrba
- EC
- 1.6.5.2
- UniProt
- P0A8G6
- Ligands
- FMN
- Pockets
- 2 · best druggability 0.61
Structure
x-ray diffraction · 1 distinct chain · 40% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | Flavoprotein wrba (EC 1.6.5.2) | protein | 197 | 40% helix, 19% strand | P0A8G6 |
Ligands and binding sites
- FMN · Flavin mononucleotide · ligand · 2 copies · chains A, C
- EDO · 1,2-ethanediol · additive · 14 copies · chains A, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 397 | 0.61 | 0.77 | 38 | EDO, FMN |
| 2 | 371 | 0.59 | 0.76 | 36 | FMN, EDO |
Interfaces
1 interface between chains.
- A–C · 872 Ų buried · 10 hydrogen bonds · protein-protein
Compared structures
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 P0A8G6
- Elsewhere: RCSB PDB 2R96 · PDBe 2R96 · UniProt P0A8G6
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