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Crystal structure of cbpf in complex with atropine by co- crystallization

Analyse Crystal structure of cbpf in complex with atropine by co- crystallization in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2X8P
Type: protein
Length: 311 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Choline-binding protein F
UniProt: Q8DR52
Ligands: CHT, OIN, SO4
Pockets: 3 · best druggability 0.45

Structure

x-ray diffraction · 1 distinct chain · 0% helix, 44% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Choline-binding protein F	protein	311	0% helix, 44% strand	Q8DR52

Ligands and binding sites

CHT · Choline ion · ligand · 5 copies · chains A
OIN · (1R,5S)-8-methyl-8-azabicyclo[3.2.1]oct-3-yl (2R)-3-hydroxy-2-phenylpropanoate · ligand · 2 copies · chains A
SO4 · Sulfate ion · ion · 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

3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	84	0.45	0.80	19	GOL
2	58	0.32	0.76	13	empty
3	55	0.31	0.76	18	empty

Compared structures

2X8P · Crystal Structure of CbpF in Complex with Atropine by Co- Crystallization · 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 Q8DR52
Elsewhere: RCSB PDB 2X8P · PDBe 2X8P · UniProt Q8DR52

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