MolNFT v1 · #164724 · protein
New antiparallel dimer of aureochrome 1A lov domain mutants from phaeodactylum tricornutum
6T73 · PTAUREO1A LOV2 domain: “New antiparallel dimer of aureochrome 1A lov domain mutants from phaeodactylum tricornutum”. X-ray diffraction, 2 ligands (FMN, CL), 9 pockets (best druggability 0.78). MolNFT v1 #164724 on GenesisL1: 3D…
- 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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