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Crystallographic structure of trimeric riboflavin synthase from brucella abortus
Analyse Crystallographic structure of trimeric riboflavin synthase from brucella abortus in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4FXU
- Type
- protein
- Length
- 560 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Riboflavin synthase subunit alpha
- EC
- 2.5.1.9
- UniProt
- G8SX20
- Pockets
- 4 · best druggability 0.78
Structure
x-ray diffraction · 3 distinct chains · 18% helix, 42% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Riboflavin synthase subunit alpha (EC 2.5.1.9) | protein | 194 | 19% helix, 44% strand | G8SX20 |
| B | Riboflavin synthase subunit alpha (EC 2.5.1.9) | protein | 169 | 19% helix, 37% strand | G8SX20 |
| C | Riboflavin synthase subunit alpha (EC 2.5.1.9) | protein | 197 | 17% helix, 45% strand | G8SX20 |
Pockets
4 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 733 | 0.78 | 0.82 | 74 | empty |
| 2 | 327 | 0.54 | 0.74 | 49 | empty |
| 3 | 240 | 0.50 | 0.75 | 32 | empty |
| 4 | 57 | 0.26 | 0.73 | 13 | empty |
Interfaces
3 interfaces between chains.
- A–B · 1254 Ų buried · 17 hydrogen bonds · protein-protein
- B–C · 1086 Ų buried · 10 hydrogen bonds · protein-protein
- A–C · 460 Ų buried · 2 hydrogen bonds · protein-protein
Compared structures
- 4FXU · Crystallographic structure of trimeric riboflavin synthase from Brucella abortus · 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 G8SX20
- Elsewhere: RCSB PDB 4FXU · PDBe 4FXU · UniProt G8SX20
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