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A novel signal transduction protein pii variant from synechococcus elongatus PCC7942 indicates a two-step process for nagk pii complex formation

Analyse A novel signal transduction protein pii variant from synechococcus elongatus… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2XBP
Type
protein
Length
113 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Nitrogen regulatory protein P-II
UniProt
P0A3F4
Ligands
ATP, MG, CL
Pockets
1 · best druggability 0.34

Structure

x-ray diffraction · 1 distinct chain · 28% helix, 35% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ANitrogen regulatory protein P-IIprotein11328% helix, 35% strandP0A3F4

Ligands and binding sites

  • ATP · Adenosine-5'-triphosphate · ligand · chains A
  • MG · Magnesium ion · metal
  • CL · Chloride ion · ion · chains A

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

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1710.340.7614empty

Compared structures

  • 2XBP · A novel signal transduction protein PII variant from Synechococcus elongatus PCC7942… · the same entry in another collection · chain A against A, TM-score 1.00
  • P0A3F4 · AlphaFold monomer V2.0 prediction for nitrogen regulatory protein P-II (P0A3F4) · a predicted model of the same protein · chain A against A, TM-score 0.86

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