GL1X · GenesisL1 explorer

Research workbench

Salmonella global domain 245

Analyse Salmonella global domain 245 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5I5D
Type
protein
Length
1,359 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Inner membrane protein yejm
UniProt
P40709
Pockets
20 · best druggability 0.69

Structure

x-ray diffraction · 4 distinct chains · 37% helix, 20% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AInner membrane protein yejmprotein33937% helix, 20% strandP40709
BInner membrane protein yejmprotein34036% helix, 20% strandP40709
CInner membrane protein yejmprotein33837% helix, 20% strandP40709
DInner membrane protein yejmprotein34237% helix, 21% strandP40709

Pockets

20 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
18280.690.7561empty
24690.670.7939empty
34060.640.7835empty
4770.620.9127empty
52980.580.7747empty

Interfaces

5 interfaces between chains.

  • B–D · 459 Ų buried · 8 hydrogen bonds · protein-protein
  • A–D · 273 Ų buried · 7 hydrogen bonds · protein-protein
  • B–C · 208 Ų buried · 1 hydrogen bond · protein-protein
  • A–B · 85 Ų buried · 0 hydrogen bonds · protein-protein
  • C–D · 26 Ų buried · 0 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 32 modified (engineered).

Compared structures

  • 5I5D · Salmonella global domain 245 · the same entry in another collection · chain D against D, TM-score 1.00
  • P40709 · AlphaFold monomer V2.0 prediction for inner membrane protein yejm (P40709) · a predicted model of the same protein · chain C against A, TM-score 0.99

Analyse

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