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Crystal structure of ctde in complex with FAD

Analyse Crystal structure of ctde in complex with FAD in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7KPQ
Type
protein
Length
383 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
FAD-dependent monooxygenase ctde
Ligands
FAD
Pockets
3 · best druggability 0.82

Structure

x-ray diffraction · 1 distinct chain · 40% helix, 28% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AFAD-dependent monooxygenase ctdeprotein38340% helix, 28% strand—

Ligands and binding sites

  • FAD · Flavin-adenine dinucleotide · 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, 1 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
110390.820.8381FAD
21170.440.7729empty
3550.250.7317empty

Compared structures

  • 7KPQ · Crystal structure of CtdE in complex with FAD · the same entry in another collection · chain A against A, TM-score 1.00

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