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F177R1 mutant of leut

Analyse F177R1 mutant of leut in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3MPN
Type: protein
Length: 505 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Transporter
UniProt: O67854
Ligands: LEU, MTN, NA, CL
Pockets: 4 · best druggability 0.72

Structure

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

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Transporter	protein	505	79% helix, 1% strand	O67854

Ligands and binding sites

LEU · Leucine · ligand · chains A
MTN · S-[(1-oxyl-2,2,5,5-tetramethyl-2,5-dihydro-1H-pyrrol-3-yl)methyl] methanesulfonothioate · ligand · chains A
NA · Sodium ion · metal · 2 copies · chains A
CL · Chloride ion · ion · chains A
BOG · octyl beta-D-glucopyranoside · additive · 6 copies · 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	616	0.72	0.79	53	empty
2	88	0.54	0.85	14	BOG
3	64	0.40	0.79	13	empty
4	110	0.38	0.74	17	empty

Modifications

Observed in the structure: 1 covalent (covalent ligand).

Compared structures

3MPN · F177R1 mutant of LeuT · 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 3MPN · PDBe 3MPN · UniProt O67854

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