MolNFT v1 · #71825 · protein

I204R1 mutant of leut

3MPQ · Transporter: “I204R1 mutant of leut”. X-ray diffraction, 4 ligands (LEU, MTN, NA), 5 pockets (best druggability 0.61). MolNFT v1 #71825 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 3MPQ
Type: protein
Length: 490 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: 5 · best druggability 0.61

Structure

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

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Transporter	protein	490	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 · 3 copies · 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	217	0.61	0.81	30	empty
2	109	0.54	0.82	21	empty
3	88	0.54	0.85	16	empty
4	75	0.41	0.78	13	empty
5	56	0.29	0.74	11	empty

Modifications

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

Compared structures

3MPQ · I204R1 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 3MPQ · PDBe 3MPQ · UniProt O67854

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