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Structure of the influenza AM2-BM2 chimeric channel

Analyse Structure of the influenza AM2-BM2 chimeric channel in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2LJB
Type: protein
Length: 120 residues
Chains: 4
Method: solution nmr
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: M2 protein, BM2 protein chimera
UniProt: Q9YP62, B4UQM4
Pockets: 1 · best druggability 0.83

Structure

solution nmr · 1 distinct chain · 80% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D	M2 protein, BM2 protein chimera	protein	30	80% helix, 0% strand	Q9YP62, B4UQM4

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	1073	0.83	0.84	82	empty

Interfaces

5 interfaces between chains.

A–D · 502 Å² buried · 1 hydrogen bond · protein-protein
B–C · 420 Å² buried · 2 hydrogen bonds · protein-protein
C–D · 398 Å² buried · 0 hydrogen bonds · protein-protein
A–B · 393 Å² buried · 0 hydrogen bonds · protein-protein
B–D · 24 Å² buried · 0 hydrogen bonds · protein-protein

Compared structures

2LJB · Structure of the influenza AM2-BM2 chimeric channel · 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 Q9YP62
Every structure of UniProt B4UQM4
Elsewhere: RCSB PDB 2LJB · PDBe 2LJB · UniProt Q9YP62 · UniProt B4UQM4

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