GL1X · GenesisL1 explorer

Research workbench

A refined NMR structure of a new phophopeptide-binding domain containing the FHA2 of RAD53

Analyse A refined NMR structure of a new phophopeptide-binding domain containing the… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1DMZ
Type
protein
Length
158 residues
Chains
1
Method
solution nmr
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Protein (protein kinase SPK1)
EC
2.7.1.-
UniProt
P22216

Structure

solution nmr · 1 distinct chain · 5% helix, 28% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AProtein (protein kinase SPK1) (EC 2.7.1.-)protein1585% helix, 28% strandP22216

Compared structures

  • 1DMZ · A refined NMR structure of a new phophopeptide-binding domain containing the FHA2 of RAD53 · the same entry in another collection · chain A against A, TM-score 1.00
  • P22216 · AlphaFold monomer V2.0 prediction for SERINE/THREONINE-protein kinase RAD53 (P22216) · a predicted model of the same protein · chain A against A, TM-score 0.80

Analyse

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