Research workbench
Structure of electron transferring flavoprotein from methylophilus methylotrophus, recognition loop removed by limited proteolysis
Analyse Structure of electron transferring flavoprotein from methylophilus… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1O97
- Type
- protein
- Length
- 566 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Electron transferring flavoprotein beta-subunit; Electron transferring flavoprotein…
- UniProt
- P53570, P53571
- Ligands
- AMP, FAD
- Pockets
- 4 · best druggability 0.80
Structure
x-ray diffraction · 2 distinct chains · 31% helix, 30% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| C | Electron transferring flavoprotein beta-subunit | protein | 251 | 33% helix, 29% strand | P53570 |
| D | Electron transferring flavoprotein alpha-subunit | protein | 315 | 29% helix, 31% strand | P53571 |
Ligands and binding sites
- AMP · Adenosine monophosphate · ligand · chains C
- FAD · Flavin-adenine dinucleotide · ligand · chains C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 595 | 0.80 | 0.86 | 62 | AMP |
| 2 | 1058 | 0.77 | 0.79 | 109 | FAD |
| 3 | 158 | 0.48 | 0.77 | 23 | empty |
| 4 | 171 | 0.47 | 0.76 | 24 | empty |
Interfaces
1 interface between chains.
- C–D · 3602 Ų buried · 65 hydrogen bonds · protein-protein
Compared structures
- 1O97 · Structure of electron transferring flavoprotein from Methylophilus methylotrophus… · the same entry in another collection · chain C against C, TM-score 1.00
- P53571 · AlphaFold monomer V2.0 prediction for electron transfer flavoprotein subunit alpha… · a predicted model of the same protein · chain D against A, TM-score 1.00
- P53570 · AlphaFold monomer V2.0 prediction for electron transfer flavoprotein subunit beta (P53570) · a predicted model of the same protein · chain C against A, TM-score 0.91
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 P53570
- Every structure of UniProt P53571
- Elsewhere: RCSB PDB 1O97 · PDBe 1O97 · UniProt P53570 · UniProt P53571
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