GL1X · GenesisL1 explorer

Research workbench

Substrate specificity and assembly of catalytic center derived from two structures of ligated uridylate kinase

Analyse Substrate specificity and assembly of catalytic center derived from two… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1UKY
Type
protein
Length
196 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Uridylate kinase
EC
2.7.4.-
UniProt
P15700
Ligands
ADP
Pockets
1 · best druggability 0.76

Structure

x-ray diffraction · 1 distinct chain · 56% helix, 13% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AUridylate kinase (EC 2.7.4.-)protein19656% helix, 13% strandP15700

Ligands and binding sites

  • ADP · Adenosine-5'-diphosphate · ligand · 2 copies · 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, 1 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
13180.760.8744ADP

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

  • 1UKY · Substrate specificity and assembly of catalytic center derived from two structures of… · the same entry in another collection · chain A against A, TM-score 1.00
  • P15700 · AlphaFold monomer V2.0 prediction for uridylate kinase (P15700) · a predicted model of the same protein · chain A 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.