GL1X · GenesisL1 explorer

Research workbench

Structure of a possible uridine kinase from bacillus stearothermophilus

Analyse Structure of a possible uridine kinase from bacillus stearothermophilus in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1RZ3
Type
protein
Length
184 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Hypothetical protein RBSTP0775
UniProt
P84134
Ligands
CA
Pockets
1 · best druggability 0.31

Structure

x-ray diffraction · 1 distinct chain · 43% helix, 23% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AHypothetical protein RBSTP0775protein18443% helix, 23% strandP84134

Ligands and binding sites

  • CA · Calcium ion · metal · chains A
  • ACT · Acetate ion · additive · chains A

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
1740.310.7420empty

Modifications

Observed in the structure: 4 modified (engineered).

Compared structures

  • 1RZ3 · Structure of a Possible Uridine Kinase from Bacillus stearothermophilus · 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.