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Solution NMR structure of TRNAPRO:MLV nucleocapsid protein (1:1) complex

Analyse Solution NMR structure of TRNAPRO:MLV nucleocapsid protein (1:1) complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2MS1
Type
protein + RNA
Length
126 residues
Chains
2
Method
solution nmr
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Nucleocapsid protein P10; Trnapro
UniProt
P03355
Ligands
ZN
Pockets
4 · best druggability 0.58

Structure

solution nmr · 2 distinct chains · 5% helix, 4% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ANucleocapsid protein P10protein555% helix, 4% strandP03355
BTrnaprorna71——

Ligands and binding sites

  • ZN · Zinc ion · metal · chains A

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
14070.580.7626empty
22670.540.7722empty
31690.440.7519empty
4810.310.7411empty

Interfaces

1 interface between chains.

  • A–B · 661 Ų buried · 18 hydrogen bonds · protein-nucleic

Compared structures

  • 2MS1 · Solution NMR structure of tRNApro:MLV Nucleocapsid Protein (1:1) Complex · the same entry in another collection · chain A against A, TM-score 1.00

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