Research workbench
Crystal structures of the synechocystis photoreceptor SLR1694 reveal distinct structural states related to signaling
Analyse Crystal structures of the synechocystis photoreceptor SLR1694 reveal distinct… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2HFN
- Type
- protein
- Length
- 1,412 residues
- Chains
- 10
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Synechocystis photoreceptor (SLR1694)
- UniProt
- P74295
- Ligands
- FMN
- Pockets
- 20 · best druggability 0.70
Structure
x-ray diffraction · 5 distinct chains · 37% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Synechocystis photoreceptor (SLR1694) | protein | 149 | 38% helix, 28% strand | P74295 |
| B, C | Synechocystis photoreceptor (SLR1694) | protein | 140 | 37% helix, 29% strand | P74295 |
| D | Synechocystis photoreceptor (SLR1694) | protein | 146 | 36% helix, 29% strand | P74295 |
| E, F, G, H, I | Synechocystis photoreceptor (SLR1694) | protein | 139 | 37% helix, 29% strand | P74295 |
| J | Synechocystis photoreceptor (SLR1694) | protein | 142 | 39% helix, 28% strand | P74295 |
Ligands and binding sites
- FMN · Flavin mononucleotide · ligand · 10 copies · chains A, B, C, D, E, F, G, H, I, J
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 15 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 577 | 0.70 | 0.79 | 61 | empty |
| 2 | 547 | 0.66 | 0.77 | 49 | empty |
| 3 | 553 | 0.65 | 0.77 | 48 | empty |
| 4 | 445 | 0.65 | 0.78 | 43 | empty |
| 5 | 116 | 0.64 | 0.88 | 20 | FMN |
Interfaces
15 interfaces between chains.
- A–B · 686 Ų buried · 13 hydrogen bonds · protein-protein
- C–D · 666 Ų buried · 11 hydrogen bonds · protein-protein
- E–F · 650 Ų buried · 10 hydrogen bonds · protein-protein
- I–J · 643 Ų buried · 12 hydrogen bonds · protein-protein
- A–C · 628 Ų buried · 17 hydrogen bonds · protein-protein
Compared structures
- 2HFN · Crystal Structures of the Synechocystis Photoreceptor Slr1694 Reveal Distinct Structural… · 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 P74295
- Elsewhere: RCSB PDB 2HFN · PDBe 2HFN · UniProt P74295
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