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Structural and functional analysis of phosphothreonine-dependent fha domain interactions

Analyse Structural and functional analysis of phosphothreonine-dependent fha domain… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3PO8
Type
protein
Length
98 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Putative uncharacterized protein TB39.8
UniProt
P71590
Ligands
PO4

Structure

x-ray diffraction · 1 distinct chain · 0% helix, 49% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
APutative uncharacterized protein TB39.8protein980% helix, 49% strandP71590

Ligands and binding sites

  • PO4 · Phosphate ion · ion · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Compared structures

  • 3PO8 · Structural and functional analysis of phosphothreonine-dependent FHA domain interactions · the same entry in another collection · chain A against A, TM-score 1.00
  • P71590 · AlphaFold monomer V2.0 prediction for fha domain-containing protein fhaa (P71590) · a predicted model of the same protein · chain A against A, TM-score 0.96

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