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Crystal structure of leut bound to L-selenomethionine in space group C2 from lipid bicelles (collected at 1.2 a)

Analyse Crystal structure of leut bound to L-selenomethionine in space group C2 from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3USM
Type: protein
Length: 502 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Transporter
UniProt: O67854
Ligands: MSE, PC, NA, IOD
Pockets: 4 · best druggability 0.69

Structure

x-ray diffraction · 1 distinct chain · 79% helix, 1% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Transporter	protein	502	79% helix, 1% strand	O67854

Ligands and binding sites

MSE · Selenomethionine · ligand · chains A
PC · Phosphocholine · ligand · chains A
NA · Sodium ion · metal · 2 copies · chains A
IOD · Iodide ion · ion · chains A

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

Pockets

4 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	568	0.69	0.78	58	empty
2	69	0.53	0.86	13	IOD
3	150	0.43	0.74	17	empty
4	98	0.40	0.76	16	empty

Compared structures

3USM · Crystal Structure of LeuT bound to L-selenomethionine in space group C2 from lipid… · 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 3USM · PDBe 3USM · UniProt O67854

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