MolNFT v1 · #169031 · protein

Cryo-EM structure of the gltph L152C-G321C mutant in the intermediate chloride conducting state.

6WYK · Glutamate transporter homolog: “Cryo-EM structure of the gltph L152C-G321C mutant in the intermediate chloride conducting state.”. Electron microscopy, 1 ligand (ASP), 7 pockets (best druggability 0.71). MolNFT v1 #169031 on…

PDB: 6WYK
Type: protein
Length: 414 residues
Chains: 1
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Glutamate transporter homolog
UniProt: O59010
Ligands: ASP
Pockets: 7 · best druggability 0.71

Structure

electron microscopy · 1 distinct chain · 79% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Glutamate transporter homolog	protein	414	79% helix, 0% strand	O59010

Ligands and binding sites

ASP · Aspartic acid · ligand · chains A

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

Pockets

7 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	81	0.71	0.95	25	empty
2	52	0.64	0.95	16	ASP
3	357	0.63	0.78	54	empty
4	228	0.52	0.76	30	empty
5	170	0.50	0.77	22	empty

Compared structures

6WYK · Cryo-EM structure of the GltPh L152C-G321C mutant in the intermediate chloride conducting… · the same entry in another collection · chain A against A, TM-score 1.00
O59010 · AlphaFold monomer V2.0 prediction for glutamate transporter homolog (O59010) · a predicted model of the same protein · chain A against A, TM-score 0.69

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 O59010
Elsewhere: RCSB PDB 6WYK · PDBe 6WYK · UniProt O59010

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