Research workbench
Structure of photolyase
Analyse Structure of photolyase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1QNF
- Type
- protein
- Length
- 475 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Photolyase
- EC
- 4.1.99.3
- UniProt
- P05327
- Ligands
- FAD, HDF
- Pockets
- 3 · best druggability 0.81
Structure
x-ray diffraction · 1 distinct chain · 52% helix, 6% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Photolyase (EC 4.1.99.3) | protein | 475 | 52% helix, 6% strand | P05327 |
Ligands and binding sites
- FAD · Flavin-adenine dinucleotide · ligand · chains A
- HDF · 8-hydroxy-10-(D-ribo-2,3,4,5-tetrahydroxypentyl)-5-deazaisoalloxazine · 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, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 712 | 0.81 | 0.85 | 60 | FAD |
| 2 | 345 | 0.75 | 0.86 | 38 | HDF |
| 3 | 114 | 0.37 | 0.74 | 22 | 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 P05327
- Elsewhere: RCSB PDB 1QNF · PDBe 1QNF · UniProt P05327
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