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Crystal structure of the drosophila CG3822 KAIR1D ligand binding domain complex with NMDA

Analyse Crystal structure of the drosophila CG3822 KAIR1D ligand binding domain complex… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5EHM
Type: protein
Length: 518 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: RE06730P,CG3822
UniProt: Q8MS48, Q9VDH5
Ligands: OEM
Pockets: 1 · best druggability 0.82

Structure

x-ray diffraction · 2 distinct chains · 37% helix, 21% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	RE06730P,CG3822	protein	261	37% helix, 21% strand	Q8MS48, Q9VDH5
B	RE06730P,CG3822	protein	257	37% helix, 21% strand	Q8MS48, Q9VDH5

Ligands and binding sites

OEM · N-methyl-D-aspartic acid · ligand · 2 copies · chains A, B

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1196	0.82	0.83	142	OEM

Interfaces

1 interface between chains.

A–B · 1027 Å² buried · 8 hydrogen bonds · protein-protein

Compared structures

5EHM · Crystal structure of the Drosophila CG3822 KaiR1D ligand binding domain complex with NMDA · 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 Q8MS48
Every structure of UniProt Q9VDH5
Elsewhere: RCSB PDB 5EHM · PDBe 5EHM · UniProt Q8MS48 · UniProt Q9VDH5

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