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Crystal structure of leut bound to L-selenomethionine in space group P21212 from lipid bicelles

Analyse Crystal structure of leut bound to L-selenomethionine in space group P21212… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3USO
Type: protein
Length: 1,004 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Transporter
UniProt: O67854
Ligands: MSE, NA
Pockets: 12 · best druggability 0.81

Structure

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

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

Ligands and binding sites

MSE · Selenomethionine · ligand · 2 copies · chains A, B
NA · Sodium ion · metal · 4 copies · chains A, B

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	227	0.81	0.93	24	empty
2	598	0.70	0.78	54	empty
3	466	0.68	0.79	45	empty
4	75	0.52	0.85	16	empty
5	75	0.52	0.85	17	empty

Interfaces

1 interface between chains.

A–B · 1121 Å² buried · 0 hydrogen bonds · protein-protein

Compared structures

3USO · Crystal structure of LeuT bound to L-selenomethionine in space group P21212 from lipid… · the same entry in another collection · chain B against B, TM-score 1.00

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Every structure of UniProt O67854
Elsewhere: RCSB PDB 3USO · PDBe 3USO · UniProt O67854

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