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Visualization of protein-nucleic acid interactions in a virus. refined structure of intact tobacco mosaic virus at 2.9 ångströms resolution by X-ray fiber diffraction

Analyse Visualization of protein-nucleic acid interactions in a virus. refined… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2TMV
Type: protein + RNA
Length: 157 residues
Chains: 2
Method: fiber diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: RNA (5'-R(P*GP*AP*A)-3'); Tmv coat protein
UniProt: P03570
Ligands: CA
Pockets: 1 · best druggability 0.70

Structure

fiber diffraction · 2 distinct chains · 45% helix, 5% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
R	RNA (5'-R(PGPAP*A)-3')	rna	3	—	—
P	Tmv coat protein	protein	154	45% helix, 5% strand	P03570

Ligands and binding sites

CA · Calcium ion · metal · chains R, P

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	50	0.70	0.98	22	empty

Interfaces

1 interface between chains.

R–P · 428 Å² buried · 9 hydrogen bonds · protein-nucleic

Compared structures

2TMV · Visualization of protein-nucleic acid interactions in a virus. refined structure of… · the same entry in another collection · chain R against R, 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 P03570
Elsewhere: RCSB PDB 2TMV · PDBe 2TMV · UniProt P03570

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