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Structure of the chromophore binding domain of bacterial phytochrome
Analyse Structure of the chromophore binding domain of bacterial phytochrome in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1ZTU
- Type
- protein
- Length
- 313 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Bacteriophytochrome
- EC
- 2.7.3.-
- UniProt
- Q9RZA4
- Ligands
- BLA
- Pockets
- 3 · best druggability 0.81
Structure
x-ray diffraction · 1 distinct chain · 30% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Bacteriophytochrome (EC 2.7.3.-) | protein | 313 | 30% helix, 27% strand | Q9RZA4 |
Ligands and binding sites
- BLA · Biliverdine IX alpha · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 446 | 0.81 | 0.89 | 65 | BLA |
| 2 | 136 | 0.50 | 0.79 | 35 | empty |
| 3 | 57 | 0.32 | 0.76 | 15 | empty |
Modifications
Observed in the structure: 5 modified, 1 cofactor (engineered, biliverdin attachment).
Compared structures
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 Q9RZA4
- Elsewhere: RCSB PDB 1ZTU · PDBe 1ZTU · UniProt Q9RZA4
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