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Crystal structure of leut-F253A bound to L-leucine from lipid bicelles

Analyse Crystal structure of leut-F253A bound to L-leucine from lipid bicelles in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4FXZ
Type: protein
Length: 502 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Transporter
UniProt: O67854
Ligands: LEU, NA
Pockets: 5 · best druggability 0.71

Structure

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

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Transporter	protein	502	78% helix, 1% strand	O67854

Ligands and binding sites

LEU · Leucine · ligand · chains A
NA · Sodium ion · metal · 2 copies · chains A
ACT · Acetate ion · additive · chains A
UND · Undecane · 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, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	454	0.71	0.81	51	LEU
2	200	0.57	0.80	27	empty
3	66	0.52	0.86	14	empty
4	97	0.44	0.78	15	empty
5	145	0.43	0.74	17	empty

Compared structures

4FXZ · Crystal structure of LeuT-F253A bound to L-leucine from lipid bicelles · 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 4FXZ · PDBe 4FXZ · UniProt O67854

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