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Solution structure of HIV-1 myrma bound to di-C4-phosphatidylinositol- (4,5)-bisphosphate

Analyse Solution structure of HIV-1 myrma bound to di-C4-phosphatidylinositol… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2H3Q
Type: protein
Length: 131 residues
Chains: 1
Method: solution nmr
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Gag polyprotein
UniProt: P12497
Ligands: MYR, PBU
Pockets: 1 · best druggability 0.30

Structure

solution nmr · 1 distinct chain · 56% helix, 2% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Gag polyprotein	protein	131	56% helix, 2% strand	P12497

Ligands and binding sites

MYR · Myristic acid · ligand · chains A
PBU · (2R)-3-{[(R)-hydroxy{[(1r,2r,3s,4r,5r,6s)-2,3,6-trihydroxy-4,5-bis(phosphonooxy) cyclohexyl]oxy}phosphoryl]oxy}propane-1,2-diyl dibutanoate · ligand · chains A

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

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	69	0.30	0.74	12	empty

Modifications

Observed in the structure: 1 lipid (myristoylation).

Compared structures

2H3Q · Solution structure of HIV-1 myrMA bound to di-C4-phosphatidylinositol-(4,5)-bisphosphate · 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 P12497
Elsewhere: RCSB PDB 2H3Q · PDBe 2H3Q · UniProt P12497

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