- PDB-2ap9: Crystal structure of acetylglutamate kinase from Mycobacterium tu... -
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Basic information
Entry
Database: PDB / ID: 2ap9
Title
Crystal structure of acetylglutamate kinase from Mycobacterium tuberculosis CDC1551
Components
acetylglutamate kinase
Keywords
SIGNALING PROTEIN / TRANSFERASE / Structural Genomics / Protein Structure Initiative / NYSGXRC / T1702 / acetylglutamate kinase / PSI / New York SGX Research Center for Structural Genomics
Function / homology
Function and homology information
acetylglutamate kinase / acetylglutamate kinase activity / acetyl-CoA:L-glutamate N-acetyltransferase activity / N-acetyl-gamma-glutamyl-phosphate reductase activity / arginine biosynthetic process via ornithine / glutamate metabolic process / arginine biosynthetic process / cell wall / arginine binding / peptidoglycan-based cell wall ...acetylglutamate kinase / acetylglutamate kinase activity / acetyl-CoA:L-glutamate N-acetyltransferase activity / N-acetyl-gamma-glutamyl-phosphate reductase activity / arginine biosynthetic process via ornithine / glutamate metabolic process / arginine biosynthetic process / cell wall / arginine binding / peptidoglycan-based cell wall / phosphorylation / ATP binding / plasma membrane / cytoplasm Similarity search - Function
Type: ADSC QUANTUM 315 / Detector: CCD / Date: Apr 7, 2005 Details: Vertical focussing mirror down stream of monochromator
Radiation
Monochromator: SAGITALLY FOCUSED Si(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelength
Wavelength: 0.975 Å / Relative weight: 1
Reflection
Resolution: 2.8→50 Å / Num. all: 94360 / Num. obs: 94360 / % possible obs: 94 % / Observed criterion σ(I): -1 / Redundancy: 3.17 % / Biso Wilson estimate: 14.5 Å2 / Rsym value: 0.083 / Net I/σ(I): 14.61
Reflection shell
Resolution: 2.8→2.9 Å / Mean I/σ(I) obs: 1.03 / Num. unique all: 6358 / Rsym value: 0.497 / % possible all: 63.5
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Processing
Software
Name
Version
Classification
DENZO
datareduction
SCALEPACK
datascaling
MLPHARE
phasing
CNS
1.1
refinement
Refinement
Method to determine structure: SAD / Resolution: 2.8→48.8 Å / Rfactor Rfree error: 0.004 / Data cutoff high absF: 178264.75 / Data cutoff low absF: 0 / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(F): 0 / Stereochemistry target values: Engh & Huber Details: Certain regions of the model do not have well defined electron density. These are residues 143-152 and 222-231. Two solvent peaks have been refined as Magnesium ions, and one solvent peak ...Details: Certain regions of the model do not have well defined electron density. These are residues 143-152 and 222-231. Two solvent peaks have been refined as Magnesium ions, and one solvent peak has be refined as a Nickle ion (as it is bound to His6 rag).
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