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NMR structure of the FHA1 domain of RAD53 in complex with a biological relevant phosphopeptide derived from MADT1

Analyse NMR structure of the FHA1 domain of RAD53 in complex with a biological relevant… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2A0T
Type
protein
Length
161 residues
Chains
2
Method
solution nmr
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
SERINE/THREONINE-protein kinase RAD53; Hypothetical 73.8 kda protein in SAS3-SEC17…
EC
2.7.1.37
UniProt
P22216, P34217

Structure

solution nmr · 2 distinct chains · 15% helix, 31% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ASERINE/THREONINE-protein kinase RAD53 (EC 2.7.1.37)protein15116% helix, 33% strandP22216
BHypothetical 73.8 kda protein in SAS3-SEC17 intergenic region, residues 301-310protein100% helix, 0% strandP34217

Interfaces

1 interface between chains.

  • A–B · 413 Ų buried · 7 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 1 modified (phosphorylation).

Compared structures

  • 2A0T · NMR structure of the FHA1 domain of Rad53 in complex with a biological relevant… · 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 0.81
  • P34217 · AlphaFold monomer V2.0 prediction for RNA-binding protein PIN4 (P34217) · a predicted model of the same protein · chain B against A, TM-score 0.37

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