Research workbench
Crystal structure analysis of synechocystis sp. PCC6803 cryptochrome
Analyse Crystal structure analysis of synechocystis sp. PCC6803 cryptochrome in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1NP7
- Type
- protein
- Length
- 966 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- DNA photolyase
- UniProt
- P77967
- Ligands
- FAD, SO4
- Pockets
- 9 · best druggability 0.82
Structure
x-ray diffraction · 1 distinct chain · 51% helix, 8% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | DNA photolyase | protein | 483 | 51% helix, 8% strand | P77967 |
Ligands and binding sites
- FAD · Flavin-adenine dinucleotide · ligand · 2 copies · chains A, B
- SO4 · Sulfate ion · ion · 3 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
9 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 605 | 0.82 | 0.87 | 53 | FAD |
| 2 | 663 | 0.81 | 0.86 | 62 | FAD |
| 3 | 232 | 0.79 | 0.93 | 40 | empty |
| 4 | 329 | 0.75 | 0.87 | 49 | empty |
| 5 | 126 | 0.49 | 0.79 | 17 | empty |
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 P77967
- Elsewhere: RCSB PDB 1NP7 · PDBe 1NP7 · UniProt P77967
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