MolNFT v1 · #93924 · protein
2.75 ångström resolution crystal structure of the a. thaliana LOV2 domain with an extended N-terminal a' helix (cryo dark structure)
4HHD · Phototropin-1: “2.75 ångström resolution crystal structure of the a. thaliana LOV2 domain with an extended N-terminal a'…”. X-ray diffraction, 2 ligands (FMN, NA), 5 pockets (best druggability 0.70). MolNFT v1 #93924 on GenesisL1…
- PDB
- 4HHD
- Type
- protein
- Length
- 304 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Phototropin-1
- EC
- 2.7.11.1
- UniProt
- O48963
- Ligands
- FMN, NA
- Pockets
- 5 · best druggability 0.70
Structure
x-ray diffraction · 2 distinct chains · 43% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Phototropin-1 (EC 2.7.11.1) | protein | 152 | 43% helix, 25% strand | O48963 |
| B | Phototropin-1 (EC 2.7.11.1) | protein | 152 | 44% helix, 24% strand | O48963 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 176 | 0.70 | 0.88 | 22 | FMN |
| 2 | 156 | 0.69 | 0.88 | 21 | FMN |
| 3 | 59 | 0.42 | 0.82 | 16 | empty |
| 4 | 64 | 0.40 | 0.80 | 21 | NA |
| 5 | 52 | 0.35 | 0.79 | 12 | empty |
Interfaces
1 interface between chains.
- A–B · 1478 Ų buried · 21 hydrogen bonds · protein-protein
Compared structures
- 4HHD · 2.75 Angstrom resolution crystal structure of the A. thaliana LOV2 domain with an… · the same entry in another collection · chain B against B, TM-score 1.00
- O48963 · AlphaFold monomer V2.0 prediction for phototropin-1 (O48963) · a predicted model of the same protein · chain B against A, TM-score 0.89
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 O48963
- Elsewhere: RCSB PDB 4HHD · PDBe 4HHD · UniProt O48963
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