Research workbench
Crystal structure of pigeon cryptochrome 4 mutant Y319D in complex with flavin adenine dinucleotide
Analyse Crystal structure of pigeon cryptochrome 4 mutant Y319D in complex with flavin… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6PTZ
- Type
- protein
- Length
- 479 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cryptochrome-1
- UniProt
- A0A2I0LZR8
- Ligands
- FAD, MG
- Pockets
- 4 · best druggability 0.78
Structure
x-ray diffraction · 1 distinct chain · 54% helix, 7% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cryptochrome-1 | protein | 479 | 54% helix, 7% strand | A0A2I0LZR8 |
Ligands and binding sites
- FAD · Flavin-adenine dinucleotide · ligand · chains A
- MG · Magnesium ion · metal · chains A
- PEG · Di(hydroxyethyl)ether · additive · 7 copies · chains A
- GOL · Glycerol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 408 | 0.78 | 0.87 | 41 | FAD, MG |
| 2 | 249 | 0.78 | 0.91 | 42 | PEG |
| 3 | 91 | 0.32 | 0.73 | 18 | empty |
| 4 | 67 | 0.29 | 0.73 | 12 | PEG |
Compared structures
- 6PTZ · Crystal structure of pigeon Cryptochrome 4 mutant Y319D in complex with flavin adenine… · 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 A0A2I0LZR8
- Elsewhere: RCSB PDB 6PTZ · PDBe 6PTZ · UniProt A0A2I0LZR8
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