Research workbench
New antiparallel dimer of aureochrome 1A lov domain mutants from phaeodactylum tricornutum
Analyse New antiparallel dimer of aureochrome 1A lov domain mutants from phaeodactylum… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6T73
- Type
- protein
- Length
- 408 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- PTAUREO1A LOV2 domain
- UniProt
- A0A140UHJ0
- Ligands
- FMN, CL
- Pockets
- 9 · best druggability 0.78
Structure
x-ray diffraction · 1 distinct chain · 36% helix, 30% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C | PTAUREO1A LOV2 domain | protein | 136 | 36% helix, 30% strand | A0A140UHJ0 |
Ligands and binding sites
- FMN · Flavin mononucleotide · ligand · 3 copies · chains A, B, C
- CL · Chloride ion · ion · 3 copies · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
9 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 83 | 0.78 | 0.98 | 20 | empty |
| 2 | 172 | 0.72 | 0.90 | 24 | FMN |
| 3 | 171 | 0.71 | 0.89 | 24 | FMN |
| 4 | 174 | 0.71 | 0.89 | 25 | FMN |
| 5 | 128 | 0.58 | 0.84 | 25 | empty |
Interfaces
3 interfaces between chains.
- A–B · 1537 Ų buried · 31 hydrogen bonds · protein-protein
- A–C · 633 Ų buried · 2 hydrogen bonds · protein-protein
- B–C · 252 Ų buried · 1 hydrogen bond · protein-protein
Compared structures
- 6T73 · New antiparallel dimer of aureochrome 1a LOV domain mutants from Phaeodactylum tricornutum · 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 A0A140UHJ0
- Elsewhere: RCSB PDB 6T73 · PDBe 6T73 · UniProt A0A140UHJ0
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