Research workbench
Mutant of class II CPD photolyase from Methanosarcina mazei
Analyse Mutant of class II CPD photolyase from Methanosarcina mazei in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5O8E
- Type
- protein
- Length
- 451 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.7
- Source
- Methanosarcina mazei Go1
- Molecule
- Deoxyribodipyrimidine photolyase
- EC
- 4.1.99.3
- UniProt
- Q8PYK9
- Ligands
- FAD, SO4
- Pockets
- 5 · best druggability 0.83
Structure
x-ray diffraction · resolution 1.7 · 1 distinct chain · 54% helix, 8% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Deoxyribodipyrimidine photolyase (EC 4.1.99.3) | protein | 451 | 54% helix, 8% strand | Q8PYK9 |
Ligands and binding sites
- FAD · Flavin-adenine dinucleotide · ligand · chains A
- SO4 · Sulfate ion · ion · 8 copies · chains A
- GOL · Glycerol · additive · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 570 | 0.83 | 0.89 | 45 | FAD, GOL |
| 2 | 375 | 0.78 | 0.88 | 45 | GOL, SO4 |
| 3 | 73 | 0.53 | 0.85 | 24 | SO4 |
| 4 | 109 | 0.43 | 0.78 | 23 | empty |
| 5 | 106 | 0.43 | 0.77 | 24 | empty |
Compared structures
- 5O8E · Mutant of class II cpd photolyase from methanosarcina mazei · 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 Q8PYK9
- Elsewhere: RCSB PDB 5O8E · PDBe 5O8E · UniProt Q8PYK9
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