Research workbench
Crystal structure of the escherichia COLI alkanesulfonate FMN reductase ssue in apo form
Analyse Crystal structure of the escherichia COLI alkanesulfonate FMN reductase ssue in… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4PTY
- Type
- protein
- Length
- 695 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- FMN reductase ssue
- EC
- 1.5.1.38
- UniProt
- P80644
- Ligands
- PO4
- Pockets
- 7 · best druggability 0.72
Structure
x-ray diffraction · 3 distinct chains · 44% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| C, B | FMN reductase ssue (EC 1.5.1.38) | protein | 173 | 44% helix, 25% strand | P80644 |
| A | FMN reductase ssue (EC 1.5.1.38) | protein | 174 | 44% helix, 24% strand | P80644 |
| D | FMN reductase ssue (EC 1.5.1.38) | protein | 175 | 43% helix, 24% strand | P80644 |
Ligands and binding sites
- PO4 · Phosphate ion · ion · 2 copies · chains A, B
- GOL · Glycerol · additive · 5 copies · chains C, D, A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 316 | 0.72 | 0.85 | 52 | GOL |
| 2 | 179 | 0.56 | 0.80 | 25 | GOL |
| 3 | 176 | 0.53 | 0.79 | 23 | GOL |
| 4 | 136 | 0.45 | 0.77 | 34 | empty |
| 5 | 138 | 0.44 | 0.76 | 33 | empty |
Interfaces
3 interfaces between chains.
- A–B · 1233 Ų buried · 16 hydrogen bonds · protein-protein
- C–A · 749 Ų buried · 9 hydrogen bonds · protein-protein
- C–D · 744 Ų buried · 15 hydrogen bonds · protein-protein
Compared structures
- 4PTY · Crystal structure of the Escherichia coli alkanesulfonate FMN reductase SsuE in apo form · the same entry in another collection · chain C against C, TM-score 1.00
- P80644 · AlphaFold monomer V2.0 prediction for FMN reductase (NADPH) (P80644) · a predicted model of the same protein · chain C against A, TM-score 0.99
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 P80644
- Elsewhere: RCSB PDB 4PTY · PDBe 4PTY · UniProt P80644
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