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Structure of the GLUA2 ntd-dimer interface mutant, T78A

Analyse Structure of the GLUA2 ntd-dimer interface mutant, T78A in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3N6V
Type: protein
Length: 2,208 residues
Chains: 6
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Glutamate receptor 2
UniProt: P19491
Pockets: 20 · best druggability 0.86

Structure

x-ray diffraction · 6 distinct chains · 34% helix, 21% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Glutamate receptor 2	protein	370	33% helix, 21% strand	P19491
B	Glutamate receptor 2	protein	372	34% helix, 21% strand	P19491
C	Glutamate receptor 2	protein	369	37% helix, 21% strand	P19491
D	Glutamate receptor 2	protein	368	34% helix, 21% strand	P19491
E	Glutamate receptor 2	protein	365	34% helix, 22% strand	P19491
F	Glutamate receptor 2	protein	364	34% helix, 20% strand	P19491

Pockets

20 pockets found on a 1 Å grid, 10 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1080	0.86	0.87	132	empty
2	998	0.86	0.87	124	empty
3	1039	0.85	0.86	108	empty
4	1028	0.73	0.76	67	empty
5	441	0.72	0.82	46	empty

Interfaces

6 interfaces between chains.

A–B · 1424 Å² buried · 12 hydrogen bonds · protein-protein
E–F · 1367 Å² buried · 10 hydrogen bonds · protein-protein
C–D · 1348 Å² buried · 6 hydrogen bonds · protein-protein
A–D · 407 Å² buried · 2 hydrogen bonds · protein-protein
A–E · 316 Å² buried · 6 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 6 disulfide (disulfide).

Compared structures

3N6V · Structure of the GluA2 NTD-dimer interface mutant, T78A · 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 3N6V · PDBe 3N6V · UniProt P19491

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