Research workbench
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).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | FAD-dependent monooxygenase ctde | protein | 383 | 40% 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.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1039 | 0.82 | 0.83 | 81 | FAD |
| 2 | 117 | 0.44 | 0.77 | 29 | empty |
| 3 | 55 | 0.25 | 0.73 | 17 | empty |
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
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Elsewhere: RCSB PDB 7KPQ · PDBe 7KPQ
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