Research workbench
E16KE61KD126KD150K flavodoxin from anabaena
Analyse E16KE61KD126KD150K flavodoxin from anabaena in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3ESX
- Type
- protein
- Length
- 337 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Flavodoxin
- UniProt
- P0A3E0
- Ligands
- FMN, CA, CL
- Pockets
- 3 · best druggability 0.53
Structure
x-ray diffraction · 2 distinct chains · 37% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Flavodoxin | protein | 168 | 39% helix, 22% strand | P0A3E0 |
| B | Flavodoxin | protein | 169 | 36% helix, 22% strand | P0A3E0 |
Ligands and binding sites
- FMN · Flavin mononucleotide · ligand · 2 copies · chains A, B
- CA · Calcium ion · metal · 3 copies · chains A, B
- CL · Chloride ion · ion · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 95 | 0.53 | 0.84 | 22 | FMN |
| 2 | 102 | 0.50 | 0.82 | 22 | FMN |
| 3 | 268 | 0.49 | 0.74 | 25 | empty |
Interfaces
1 interface between chains.
- A–B · 170 Ų buried · 1 hydrogen bond · 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 P0A3E0
- Elsewhere: RCSB PDB 3ESX · PDBe 3ESX · UniProt P0A3E0
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