Research workbench

Gltph in complex with L-aspartate and sodium ions in outward-facing state

Analyse Gltph in complex with L-aspartate and sodium ions in outward-facing state in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6UWF
Type: protein
Length: 416 residues
Chains: 1
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Glutamate transporter homolog
Ligands: 6OU, ASP
Pockets: 3 · best druggability 0.45

Structure

electron microscopy · 1 distinct chain · 76% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Glutamate transporter homolog	protein	416	76% helix, 0% strand	—

Ligands and binding sites

6OU · [(2~{R})-1-[2-azanylethoxy(oxidanyl)phosphoryl]oxy-3-hexadecanoyloxy-propan-2-yl] (~{Z})-octadec-9-enoate · ligand · 2 copies · chains A
ASP · Aspartic acid · ligand · chains A

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

Pockets

3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	212	0.45	0.73	27	6OU
2	63	0.30	0.74	17	empty
3	65	0.29	0.72	16	empty

Modifications

Observed in the structure: 1 covalent, 1 modified (covalent ligand, formylation).

Compared structures

6UWF · GltPh in complex with L-aspartate and sodium ions in outward-facing state · 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
Elsewhere: RCSB PDB 6UWF · PDBe 6UWF

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