Research workbench

Crystal structure of cbpf in complex with ipratropium by soaking

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

PDB: 2X8M
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, X8M, SO4
Pockets: 3 · best druggability 0.41

Structure

x-ray diffraction · 1 distinct chain · 0% helix, 45% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Choline-binding protein F	protein	311	0% helix, 45% strand	Q8DR52

Ligands and binding sites

CHT · Choline ion · ligand · 6 copies · chains A
X8M · Ipratropium · ligand · 3 copies · chains A
SO4 · Sulfate ion · ion · chains A
GOL · Glycerol · additive · 6 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	53	0.41	0.82	16	GOL
2	53	0.32	0.77	14	empty
3	53	0.31	0.76	16	empty

Compared structures

2X8M · Crystal Structure of CbpF in complex with ipratropium by soaking · 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 2X8M · PDBe 2X8M · UniProt Q8DR52

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