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Crystal structure of carnitine transporter from proteus mirabilis

Analyse Crystal structure of carnitine transporter from proteus mirabilis in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2WSW
Type: protein
Length: 508 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Bcct family BETAINE/CARNITINE/CHOLINE transporter
UniProt: C2LLR0
Ligands: CM5
Pockets: 5 · best druggability 0.79

Structure

x-ray diffraction · 1 distinct chain · 78% helix, 1% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Bcct family BETAINE/CARNITINE/CHOLINE transporter	protein	508	78% helix, 1% strand	C2LLR0

Ligands and binding sites

CM5 · 5-cyclohexyl-1-pentyl-beta-D-maltoside · ligand · chains A
GOL · Glycerol · additive · chains A
1PE · Pentaethylene glycol · additive · chains A

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

Pockets

5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	956	0.79	0.81	69	GOL, 1PE
2	234	0.63	0.81	29	empty
3	103	0.45	0.79	22	empty
4	100	0.37	0.75	19	empty
5	50	0.26	0.74	10	empty

Compared structures

2WSW · Crystal Structure of Carnitine Transporter from Proteus mirabilis · 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 C2LLR0
Elsewhere: RCSB PDB 2WSW · PDBe 2WSW · UniProt C2LLR0

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