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Crystal structure of cmer bound to taurocholic acid

Analyse Crystal structure of cmer bound to taurocholic acid in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3HGY
Type: protein
Length: 202 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cmer
UniProt: Q7B8P6
Ligands: TCH
Pockets: 1 · best druggability 0.71

Structure

x-ray diffraction · 1 distinct chain · 73% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Cmer	protein	202	73% helix, 0% strand	Q7B8P6

Ligands and binding sites

TCH · Taurocholic acid · ligand · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	432	0.71	0.81	33	TCH

Compared structures

3HGY · Crystal Structure of CmeR Bound to Taurocholic Acid · 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 Q7B8P6
Elsewhere: RCSB PDB 3HGY · PDBe 3HGY · UniProt Q7B8P6

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