GL1X · GenesisL1 explorer

Research workbench

Crystal structure of bacillus cereus tubz, apo-form

Analyse Crystal structure of bacillus cereus tubz, apo-form in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4EI8
Type
protein
Length
360 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Plasmid replication protein repx
UniProt
Q74P24
Pockets
3 · best druggability 0.45

Structure

x-ray diffraction · 1 distinct chain · 44% helix, 21% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
APlasmid replication protein repxprotein36044% helix, 21% strandQ74P24

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11440.450.7726empty
21210.390.7422empty
3680.370.7819empty

Modifications

Observed in the structure: 4 modified (engineered).

Compared structures

  • 4EI8 · Crystal structure of Bacillus cereus TubZ, apo-form · the same entry in another collection · chain A against A, TM-score 1.00
  • Q74P24 · AlphaFold monomer V2.0 prediction for tubulin-like protein tubz (Q74P24) · a predicted model of the same protein · chain A against A, TM-score 0.94

Analyse

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