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Structural basis of the nucleotide driven conformational changes in the aaa domain of transcription activator pspf

Analyse Structural basis of the nucleotide driven conformational changes in the aaa… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2C99
Type
protein
Length
243 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Psp operon transcriptional activator
UniProt
P37344
Ligands
ANP
Pockets
3 · best druggability 0.44

Structure

x-ray diffraction · 1 distinct chain · 47% helix, 13% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
APsp operon transcriptional activatorprotein24347% helix, 13% strandP37344

Ligands and binding sites

  • ANP · Phosphoaminophosphonic acid-adenylate ester · ligand · chains A

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11160.440.7721ANP
2680.390.7915empty
3890.370.7617empty

Compared structures

  • 2C99 · Structural basis of the nucleotide driven conformational changes in the AAA domain of… · the same entry in another collection · chain A against A, TM-score 1.00
  • P37344 · AlphaFold monomer V2.0 prediction for psp operon transcriptional activator (P37344) · a predicted model of the same protein · chain A against A, TM-score 0.95

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