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Solution structure of the FHA2 domain of RAD53 complexed with a phosphothreonyl peptide derived from RAD9

Analyse Solution structure of the FHA2 domain of RAD53 complexed with a phosphothreonyl… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1K2N
Type
protein
Length
167 residues
Chains
2
Method
solution nmr
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Protein kinase SPK1; DNA repair protein RAD9
EC
2.7.1.-
UniProt
P22216, P14737

Structure

solution nmr · 2 distinct chains · 5% helix, 33% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AProtein kinase SPK1 (EC 2.7.1.-)protein1585% helix, 35% strandP22216
PDNA repair protein RAD9protein90% helix, 0% strandP14737

Interfaces

1 interface between chains.

  • A–P · 422 Ų buried · 7 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 1 modified (phosphorylation).

Compared structures

  • 1K2N · Solution Structure of the FHA2 domain of Rad53 Complexed with a Phosphothreonyl Peptide… · 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 0.84
  • P14737 · AlphaFold monomer V2.0 prediction for DNA repair protein RAD9 (P14737) · a predicted model of the same protein · chain P against A, TM-score 0.50

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