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Crystal structure of leut in heptyl-beta-D-selenoglucoside

Analyse Crystal structure of leut in heptyl-beta-D-selenoglucoside in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3USP
Type: protein
Length: 503 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Transporter
UniProt: O67854
Ligands: 05L, LEU, NA, CL
Pockets: 6 · best druggability 0.64

Structure

x-ray diffraction · 1 distinct chain · 77% helix, 1% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Transporter	protein	503	77% helix, 1% strand	O67854

Ligands and binding sites

05L · heptyl 1-seleno-beta-D-glucopyranoside · ligand · 9 copies · chains A
LEU · Leucine · ligand · chains A
NA · Sodium ion · metal · 2 copies · chains A
CL · Chloride ion · ion · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	305	0.64	0.80	32	05L
2	142	0.56	0.82	23	empty
3	96	0.54	0.84	16	empty
4	72	0.40	0.78	13	empty
5	50	0.38	0.80	12	empty

Compared structures

3USP · Crystal structure of LeuT in heptyl-beta-D-Selenoglucoside · 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 O67854
Elsewhere: RCSB PDB 3USP · PDBe 3USP · UniProt O67854

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