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X-ray structure of the GLUR2 ligand binding core (S1S2J) in complex with br-hibo at 1.65 a resolution

Analyse X-ray structure of the GLUR2 ligand binding core (S1S2J) in complex with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1M5C
Type: protein
Length: 258 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Glutamate receptor 2
UniProt: P19491
Ligands: BRH
Pockets: 4 · best druggability 0.69

Structure

x-ray diffraction · 1 distinct chain · 37% helix, 21% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Glutamate receptor 2	protein	258	37% helix, 21% strand	P19491

Ligands and binding sites

BRH · (S)-2-amino-3-(4-bromo-3-hydroxy-isoxazol-5-yl)propionic acid · ligand · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	57	0.69	0.97	17	BRH
2	100	0.36	0.74	24	empty
3	69	0.31	0.75	16	empty
4	51	0.26	0.73	11	empty

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

1M5C · X-RAY STRUCTURE OF THE GLUR2 LIGAND BINDING CORE (S1S2J) IN COMPLEX WITH Br-HIBO AT 1.65… · 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 P19491
Elsewhere: RCSB PDB 1M5C · PDBe 1M5C · UniProt P19491

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