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Crystal structure of leut bound to L-selenomethionine and sodium

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

PDB: 3F4I
Type: protein
Length: 509 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Transporter
UniProt: O67854
Ligands: MSE, NA
Pockets: 5 · best druggability 0.71

Structure

x-ray diffraction · 1 distinct chain · 77% helix, 1% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Transporter	protein	509	77% helix, 1% strand	O67854

Ligands and binding sites

MSE · Selenomethionine · ligand · chains A
NA · Sodium ion · metal · 2 copies · chains A
BOG · octyl beta-D-glucopyranoside · additive · 5 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, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	605	0.71	0.78	51	empty
2	100	0.54	0.84	16	empty
3	73	0.41	0.79	12	empty
4	50	0.37	0.80	11	empty
5	91	0.35	0.74	13	empty

Compared structures

3F4I · Crystal Structure of LeuT bound to L-selenomethionine and sodium · 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 3F4I · PDBe 3F4I · UniProt O67854

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