MolNFT v1 · #51231 · protein
N- and C-terminal helices of oat LOV2 (404-546) are involved in light- induced signal transduction (room temperature (293K) light structure of LOV2 (404-546))
2V1B · NPH1-1: “N- and C-terminal helices of oat LOV2 (404-546) are involved in light- induced signal transduction (room…”. X-ray diffraction, 1 ligand (FMN), 1 pocket (best druggability 0.72). MolNFT v1 #51231 on GenesisL1: 3D structure…
- PDB
- 2V1B
- Type
- protein
- Length
- 144 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- NPH1-1
- UniProt
- O49003
- Ligands
- FMN
- Pockets
- 1 · best druggability 0.72
Structure
x-ray diffraction · 1 distinct chain · 36% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | NPH1-1 | protein | 144 | 36% helix, 27% strand | O49003 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 143 | 0.72 | 0.91 | 22 | FMN |
Modifications
Observed in the structure: 1 cofactor (flavinylation).
Compared structures
- 2V1B · N- and C-terminal helices of oat LOV2 (404-546) are involved in light-induced signal… · 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 O49003
- Elsewhere: RCSB PDB 2V1B · PDBe 2V1B · UniProt O49003
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