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Crystal structure of gltph fast mutant - R276S/M395R

Analyse Crystal structure of gltph fast mutant - R276S/M395R in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6CTF
Type
protein
Length
1,233 residues
Chains
3
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Glutamate transporter homolog
UniProt
O59010
Ligands
ASP, NA
Pockets
18 · best druggability 0.87

Structure

x-ray diffraction · 1 distinct chain · 75% helix, 0% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, CGlutamate transporter homologprotein41175% helix, 0% strandO59010

Ligands and binding sites

  • ASP · Aspartic acid · ligand · 3 copies · chains A, B, C
  • NA · Sodium ion · metal · 6 copies · chains A, B, C

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

Pockets

18 pockets found on a 1 Å grid, 11 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
17620.870.9048empty
26840.690.7789empty
35640.650.7673empty
43930.640.7852empty
53870.620.7745empty

Interfaces

3 interfaces between chains.

  • A–C · 1095 Ų buried · 11 hydrogen bonds · protein-protein
  • B–C · 1059 Ų buried · 12 hydrogen bonds · protein-protein
  • A–B · 1054 Ų buried · 11 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 3 disulfide (disulfide).

Compared structures

  • 6CTF · Crystal structure of GltPh fast mutant - R276S/M395R · the same entry in another collection · chain B against B, TM-score 1.00
  • O59010 · AlphaFold monomer V2.0 prediction for glutamate transporter homolog (O59010) · a predicted model of the same protein · chain C against A, TM-score 0.64

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