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NMR structure of the SARS coronavirus E protein pentameric ion channel

Analyse NMR structure of the SARS coronavirus E protein pentameric ion channel in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5X29
Type: protein
Length: 290 residues
Chains: 5
Method: solution nmr
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Envelope small membrane protein
UniProt: P59637
Pockets: 4 · best druggability 0.78

Structure

solution nmr · 1 distinct chain · 62% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D, E	Envelope small membrane protein	protein	58	62% helix, 0% strand	P59637

Pockets

4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	474	0.78	0.84	36	empty
2	447	0.64	0.77	46	empty
3	85	0.49	0.82	14	empty
4	60	0.43	0.82	14	empty

Interfaces

5 interfaces between chains.

D–E · 567 Å² buried · 2 hydrogen bonds · protein-protein
C–D · 556 Å² buried · 1 hydrogen bond · protein-protein
A–B · 547 Å² buried · 2 hydrogen bonds · protein-protein
B–C · 522 Å² buried · 0 hydrogen bonds · protein-protein
A–E · 476 Å² buried · 1 hydrogen bond · protein-protein

Compared structures

5X29 · NMR structure of the SARS Coronavirus E protein pentameric ion 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 P59637
Elsewhere: RCSB PDB 5X29 · PDBe 5X29 · UniProt P59637

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