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Crystal structure of the E290S mutant of leut with bound og

Analyse Crystal structure of the E290S mutant of leut with bound og in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3GJC
Type: protein
Length: 996 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Transporter
UniProt: O67854
Ligands: LEU, NA
Pockets: 18 · best druggability 0.78

Structure

x-ray diffraction · 1 distinct chain · 75% helix, 1% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Transporter	protein	498	75% helix, 1% strand	O67854

Ligands and binding sites

LEU · Leucine · ligand · 2 copies · chains A, B
NA · Sodium ion · metal · 2 copies · chains A, B
BOG · octyl beta-D-glucopyranoside · additive · 8 copies · chains A, B

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

Pockets

18 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	135	0.78	0.95	22	empty
2	486	0.69	0.79	48	BOG
3	439	0.69	0.80	52	BOG
4	171	0.58	0.81	19	BOG
5	155	0.55	0.80	15	BOG

Interfaces

1 interface between chains.

A–B · 1222 Å² buried · 0 hydrogen bonds · protein-protein

Compared structures

3GJC · Crystal Structure of the E290S mutant of LeuT with bound OG · 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 3GJC · PDBe 3GJC · UniProt O67854

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