Nov 24, 2010 · 3PPO Structures of the substrate-binding protein provide insights into the multiple compatible solutes binding specificities of Bacillus subtilis ABC transporter OpuC. PDB DOI: https://doi.org/10.2210/pdb3PPO/pdb; Classification: TRANSPORT PROTEIN; Organism(s): Bacillus subtilis; Expression System: Escherichia coli; Mutation(s): No

3PPO: Structures of the substrate-binding protein provide insights into the multiple compatible solutes binding specificities of Bacillus subtilis ABC transporter OpuC

6-Phosphofructo-2-kinase/fructose-2,6-bisphosphatase isoform 3 (PFKFB3) is a key enzyme of the glycolytic pathway, and it plays an essential role in angiogenesis. 3- (3-Pyridinyl)-1- (4-pyridinyl)-2-propen-1-one (3PO) is frequently used as a glycolysis inhibitor and is …

3PPO: Structures of the substrate-binding protein provide insights into the multiple compatible solutes binding specificities of Bacillus subtilis ABC transporter OpuC

May 11, 2011 · 3ppo: Structures of the substrate-binding protein provide insights into the multiple compatible solute binding specificities of the Bacillus subtilis ABC transporter OpuC.

3PPO . DCK; DCK: (2S)-3-carboxy-2-hydroxy-N,N,N-trimethylpropan-1-aminium. Ligand Definition and Summary of DCK. DCK is a Ligand Of Interest in 3PPO designated by the RCSB. Help . Best-fitted instance in this entry: Other instances in …

3ppo is a 2 chain structure with sequence from "vibrio_subtilis"_ehrenberg_1835 "vibrio subtilis" ehrenberg 1835. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.

Nov 24, 2010 · PDB Entry - 3PPO (Status - Released) Summary information: Title: Structures of the substrate-binding protein provide insights into the multiple compatible solutes binding specificities of Bacillus subtilis ABC transporter OpuC. PDB DOI: https://doi.org/10.2210/pdb3ppo/pdb. Primary publication DOI: https://doi.org/10.1042/BJ20102097

Jun 1, 2011 · Comparative structural analysis revealed a plastic pocket that fits various compatible solutes, which attributes themultiple-substrate binding property to OpuCC. This plasticity is a gain-of-function via a single-residue mutation of Thr⁹⁴ in OpuCC compared with Asp⁹⁶ in OpuBC.

3d structure of chain 3ppo_a - structures of the substrate-binding protein provide insights into the multiple compatible solutes binding specificities of bacillus subtilis abc transporter opuc - 3ppo | cansar.ai