Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

2QMH

structure of V267F mutant HprK/P

Summary for 2QMH
Entry DOI10.2210/pdb2qmh/pdb
Related1JB1 1KKL 1KKM
DescriptorHPr kinase/phosphorylase (2 entities in total)
Functional Keywordsv267f mutation, atp-binding, carbohydrate metabolism, kinase, magnesium, metal-binding, multifunctional enzyme, nucleotide-binding, serine/threonine-protein kinase, transferase, metal binding protein
Biological sourceLactobacillus casei
Total number of polymer chains12
Total formula weight272732.34
Authors
Chaptal, V.,Vincent, F.,Gueguen-Chaignon, V.,Poncet, S.,Deutscher, J.,Nessler, S.,Morera, S. (deposition date: 2007-07-16, release date: 2007-09-18, Last modification date: 2023-08-30)
Primary citationChaptal, V.,Vincent, F.,Gueguen-Chaignon, V.,Monedero, V.,Poncet, S.,Deutscher, J.,Nessler, S.,Morera, S.
Structural Analysis of the Bacterial HPr Kinase/Phosphorylase V267F Mutant Gives Insights into the Allosteric Regulation Mechanism of This Bifunctional Enzyme.
J.Biol.Chem., 282:34952-34957, 2007
Cited by
PubMed: 17878158
DOI: 10.1074/jbc.M705979200
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.6 Å)
Structure validation

218853

PDB entries from 2024-04-24

PDB statisticsPDBj update infoContact PDBjnumon