Research workbench
Wrba from escherichia COLI, second crystal form
Analyse Wrba from escherichia COLI, second crystal form in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3B6M
- Type
- protein
- Length
- 377 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Flavoprotein wrba
- UniProt
- P0A8G6
- Ligands
- FMN
- Pockets
- 2 · best druggability 0.41
Structure
x-ray diffraction · 2 distinct chains · 41% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Flavoprotein wrba | protein | 188 | 42% helix, 20% strand | P0A8G6 |
| B | Flavoprotein wrba | protein | 189 | 39% helix, 20% strand | P0A8G6 |
Ligands and binding sites
- FMN · Flavin mononucleotide · ligand · 2 copies · chains A, B
- 144 · Tris-hydroxymethyl-methyl-ammonium · additive · 2 copies · chains A, B
- 15P · Polyethylene glycol (N=34) · additive · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 80 | 0.41 | 0.79 | 16 | FMN |
| 2 | 101 | 0.40 | 0.77 | 21 | FMN |
Interfaces
1 interface between chains.
- A–B · 1132 Ų buried · 9 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 3B6M · PDBe 3B6M · UniProt P0A8G6
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