› 3poa

X-ray diffraction
2.01Å resolution

Structural and functional analysis of phosphothreonine-dependent FHA domain interactions

Released:
DOI: 10.2210/pdb3poa/pdb
PDB entry 3poa coloured by chain, front view.
PDB entry 3poa coloured by chain, side view.
PDB entry 3poa coloured by chain, top view.
Source organism: Mycobacterium tuberculosis
Primary publication:
Structural and functional analysis of phosphothreonine-dependent FHA domain interactions.
Pennell S, Westcott S, Ortiz-Lombardía M, Patel D, Li J, Nott TJ, Mohammed D, Buxton RS, Yaffe MB, Verma C, Smerdon SJ
Structure 18 1587-95 (2010)
PMID: 21134638

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-159804 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
FHA domain-containing protein FhaA Chain: A
Molecule details ›
Chain: A
Length: 100 amino acids
Theoretical weight: 10.95 KDa
Source organism: Mycobacterium tuberculosis
Expression system: Escherichia coli
UniProt:
  • Canonical: P71590 (Residues: 431-527; Coverage: 18%)
Gene names: Rv0020c, TB39.8, fhaA
Sequence domains: FHA domain
Structure domains: Tumour Suppressor Smad4
synthetic phosphopeptide Chain: B
Molecule details ›
Chain: B
Length: 12 amino acids
Theoretical weight: 1.45 KDa
Source organism: Mycobacterium tuberculosis
Expression system: Not provided

Ligands and Environments

1 bound ligand:
Ligand ZN 1 x ZN
1 modified residue:
Ligand TPO 1 x TPO

Experiments and Validation Details

Entry percentile scores
X-ray source: SRS BEAMLINE PX14.1
Spacegroup: C2221
Unit cell:
a: 57.016Å b: 74.425Å c: 63.016Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.182 0.179 0.237
Expression systems:
  • Escherichia coli
  • Not provided

Quick links

Citations

4 review citations

Modular peptide binding: from a comparison of natural binders to designed armadillo repeat proteins.
Reichen et al. (2014)
3 more

2 mentions without citation

Dimerization Mediated by a Divergent Forkhead-associated Domain Is Essential for the DNA Damage and Spindle Functions of Fission Yeast Mdb1.
Luo et al. (2015)
1 more