› 2a0t

Solution NMR

NMR structure of the FHA1 domain of Rad53 in complex with a biological relevant phosphopeptide derived from Madt1

Released:
DOI: 10.2210/pdb2a0t/pdb
PDB entry 2a0t coloured by chain, ensemble of 20 models, front view.
PDB entry 2a0t coloured by chain, ensemble of 20 models, side view.
PDB entry 2a0t coloured by chain, ensemble of 20 models, top view.
Source organisms:
Primary publication:
FHA domain-ligand interactions: importance of integrating chemical and biological approaches.
Mahajan A, Yuan C, Pike BL, Heierhorst J, Chang CF, Tsai MD
J Am Chem Soc 127 14572-3 (2005)
PMID: 16231900

Function and Biology Details

Reaction catalysed: 
ATP + L-seryl/L-threonyl/L-tyrosyl-[protein] = ADP + O-phospho-L-seryl/O-phospho-L-threonyl/O-phospho-L-tyrosyl-[protein]
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-149542 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Serine/threonine-protein kinase RAD53 Chain: A
Molecule details ›
Chain: A
Length: 151 amino acids
Theoretical weight: 17.09 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P22216 (Residues: 14-164; Coverage: 18%)
Gene names: MEC2, P2588, RAD53, SAD1, SPK1, YPL153C
Sequence domains: FHA domain
Structure domains: Tumour Suppressor Smad4
RNA-binding protein PIN4 Chain: B
Molecule details ›
Chain: B
Length: 10 amino acids
Theoretical weight: 1.25 KDa
Source organism: Saccharomyces cerevisiae S288C
Expression system: Not provided
UniProt:
  • Canonical: P34217 (Residues: 301-310; Coverage: 2%)
Gene names: MDT1, PIN4, YBL0506, YBL0516, YBL051C

Ligands and Environments

No bound ligands
1 modified residue:
Ligand TPO 1 x TPO

Experiments and Validation Details

Entry percentile scores
Refinement method: simulated annealing
Expression systems:
  • Escherichia coli BL21(DE3)
  • Not provided

Quick links

Citations

2 review citations

Mechanistic insights into phosphoprotein-binding FHA domains.
Liang et al. (2008)
1 more

1 mention without citation

Achieving peptide binding specificity and promiscuity by loops: case of the forkhead-associated domain.
Huang et al. (2014)