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Crystal structure of N-myristoylated mouse mammary tumor virus matrix protein

Analyse Crystal structure of N-myristoylated mouse mammary tumor virus matrix protein in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4ZV5
Type
protein
Length
182 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Matrix protein P10
UniProt
P10258
Ligands
MYR
Pockets
1 · best druggability 0.81

Structure

x-ray diffraction · 1 distinct chain · 70% helix, 0% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BMatrix protein P10protein9170% helix, 0% strandP10258

Ligands and binding sites

  • MYR · Myristic acid · ligand · 2 copies · chains A, B

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.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
13480.810.9037MYR

Interfaces

1 interface between chains.

  • A–B · 851 Ų buried · 8 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 lipid (myristoylation).

Compared structures

  • 4ZV5 · Crystal structure of N-myristoylated mouse mammary tumor virus matrix protein · the same entry in another collection · chain A against A, TM-score 1.00

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