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P1/MAHONEY poliovirus, mutant P1095S

Analyse P1/MAHONEY poliovirus, mutant P1095S in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1AR8
Type
protein
Length
854 residues
Chains
5
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
P1/MAHONEY poliovirus
UniProt
P03300, P03299
Ligands
SPH, MYR
Pockets
12 · best druggability 0.79

Structure

x-ray diffraction · 5 distinct chains · 11% helix, 32% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
0P1/MAHONEY poliovirusprotein80% helix, 25% strand—
1P1/MAHONEY poliovirusprotein28310% helix, 31% strandP03300
2P1/MAHONEY poliovirusprotein26813% helix, 37% strandP03300
3P1/MAHONEY poliovirusprotein23510% helix, 30% strandP03300
4P1/MAHONEY poliovirusprotein6012% helix, 17% strandP03299

Ligands and binding sites

  • SPH · Sphingosine · ligand · chains 1, 3
  • MYR · Myristic acid · ligand · chains 0, 4

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
16920.790.8483SPH
21290.450.7729empty
32210.450.7332empty
4720.420.8014empty
5520.380.8120empty

Interfaces

7 interfaces between chains.

  • 1–3 · 3949 Ų buried · 71 hydrogen bonds · protein-protein
  • 1–2 · 2409 Ų buried · 39 hydrogen bonds · protein-protein
  • 2–3 · 1657 Ų buried · 17 hydrogen bonds · protein-protein
  • 1–4 · 1172 Ų buried · 18 hydrogen bonds · protein-protein
  • 3–4 · 850 Ų buried · 15 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 1 lipid (myristoylation).

Compared structures

  • 1AR8 · P1/MAHONEY poliovirus, mutant P1095S · the same entry in another collection · chain 2 against 2, TM-score 1.00

Analyse

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