Research workbench

Crystal structure of DNA photolyase from thermus thermophilus

Analyse Crystal structure of DNA photolyase from thermus thermophilus in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1IQR
Type: protein
Length: 415 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Photolyase
EC: 4.1.99.3
UniProt: P61497
Ligands: FAD, PO4
Pockets: 4 · best druggability 0.83

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	415	52% helix, 6% strand	P61497

Ligands and binding sites

FAD · Flavin-adenine dinucleotide · ligand · chains A
PO4 · Phosphate ion · ion · 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.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	510	0.83	0.89	47	FAD
2	757	0.81	0.84	61	PO4
3	79	0.33	0.74	19	empty
4	65	0.30	0.74	15	empty

Compared structures

1IQR · Crystal structure of DNA photolyase from Thermus thermophilus · the same entry in another collection · chain A against A, TM-score 1.00
P61497 · AlphaFold monomer V2.0 prediction for deoxyribodipyrimidine photo- lyase (P61497) · a predicted model of the same protein · chain A against A, TM-score 0.99

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 P61497
Elsewhere: RCSB PDB 1IQR · PDBe 1IQR · UniProt P61497

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.