GL1X · GenesisL1 explorer

Research workbench

Structure of the periplasmic domain of the motb L119P mutant from salmonella (crystal form 1)

Analyse Structure of the periplasmic domain of the motb L119P mutant from salmonella… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5Y3Z
Type
protein
Length
283 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Motility protein B
UniProt
P55892
Ligands
ARG
Pockets
6 · best druggability 0.72

Structure

x-ray diffraction · 2 distinct chains · 32% helix, 24% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AMotility protein Bprotein14133% helix, 23% strandP55892
BMotility protein Bprotein14230% helix, 25% strandP55892

Ligands and binding sites

  • ARG · Arginine · ligand · 3 copies · chains A, B
  • MPD · (4S)-2-methyl-2,4-pentanediol · additive · 3 copies · chains A, B
  • IMD · Imidazole · additive · 2 copies · chains A, B

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12730.720.8632IMD
21090.660.9029IMD
3640.440.8217empty
4600.340.7820empty
5720.340.7623empty

Interfaces

1 interface between chains.

  • A–B · 1386 Ų buried · 25 hydrogen bonds · protein-protein

Compared structures

  • 5Y3Z · Structure of the periplasmic domain of the MotB L119P mutant from Salmonella (crystal… · the same entry in another collection · chain B against B, TM-score 1.00
  • P55892 · AlphaFold monomer V2.0 prediction for motility protein B (P55892) · a predicted model of the same protein · chain A against A, TM-score 0.89

Analyse

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.