GL1X · GenesisL1 explorer

MolNFT v1 · #46411 · protein

Crystal structure of a DUF1048 protein with a left-handed superhelix fold (BCE_3448) from bacillus cereus atcc 10987 at 2.05 a resolution

2O3L · Hypothetical protein: “Crystal structure of a DUF1048 protein with a left-handed superhelix fold (BCE_3448) from bacillus cereus…”. X-ray diffraction, 1 ligand (SO4), 1 pocket (best druggability 0.47). MolNFT v1 #46411 on GenesisL1…

PDB
2O3L
Type
protein
Length
164 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Hypothetical protein
UniProt
Q734F7
Ligands
SO4
Pockets
1 · best druggability 0.47

Structure

x-ray diffraction · 2 distinct chains · 78% helix, 0% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AHypothetical proteinprotein8382% helix, 0% strandQ734F7
BHypothetical proteinprotein8174% helix, 0% strandQ734F7

Ligands and binding sites

  • SO4 · Sulfate ion · ion · chains B
  • GOL · Glycerol · additive · 3 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, 0 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1650.470.8420empty

Interfaces

1 interface between chains.

  • A–B · 821 Ų buried · 6 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 12 modified (engineered).

Compared structures

  • 2O3L · Crystal structure of a duf1048 protein with a left-handed superhelix fold (bce_3448) from… · the same entry in another collection · chain A against A, TM-score 1.00

Analyse

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