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- PDB-2j5v: GLUTAMATE 5-KINASE FROM ESCHERICHIA COLI COMPLEXED WITH GLUTAMYL-... -
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Open data
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Basic information
Entry | Database: PDB / ID: 2j5v | ||||||
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Title | GLUTAMATE 5-KINASE FROM ESCHERICHIA COLI COMPLEXED WITH GLUTAMYL-5-PHOSPHATE AND PYROGLUTAMIC ACID | ||||||
![]() | GLUTAMATE 5-KINASE | ||||||
![]() | TRANSFERASE / PROLINE BIOSYNTHESIS / GAMMA GLUTAMYL KINASE / AMINO-ACID BIOSYNTHESIS / GLUTAMATE KINASE / KINASE / FEEDBACK REGULATION / GLUTAMATE 5-KINASE / PUA DOMAIN / AMINO ACID KINASE / GLUTAMATE / GLUTAMYL PHOSPHATE / GAMMA GLUTAMYL PHOSPHATE / PROLINE | ||||||
Function / homology | ![]() proline binding / glutamate 5-kinase / glutamate 5-kinase activity / L-proline biosynthetic process / proline biosynthetic process / phosphorylation / magnesium ion binding / protein homodimerization activity / RNA binding / ATP binding ...proline binding / glutamate 5-kinase / glutamate 5-kinase activity / L-proline biosynthetic process / proline biosynthetic process / phosphorylation / magnesium ion binding / protein homodimerization activity / RNA binding / ATP binding / identical protein binding / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Marco-Marin, C. / Gil-Ortiz, F. / Perez-Arellano, I. / Cervera, J. / Fita, I. / Rubio, V. | ||||||
![]() | ![]() Title: A Novel Two-Domain Architecture within the Amino Acid Kinase Enzyme Family Revealed by the Crystal Structure of Escherichia Coli Glutamate 5-Kinase. Authors: Marco-Marin, C. / Gil-Ortiz, F. / Perez-Arellano, I. / Cervera, J. / Fita, I. / Rubio, V. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 137.7 KB | Display | ![]() |
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PDB format | ![]() | 106.3 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 482.9 KB | Display | ![]() |
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Full document | ![]() | 493.5 KB | Display | |
Data in XML | ![]() | 26.9 KB | Display | |
Data in CIF | ![]() | 37.2 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 2j5tC ![]() 2akoS C: citing same article ( S: Starting model for refinement |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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Unit cell |
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Noncrystallographic symmetry (NCS) | NCS domain:
NCS domain segments: Component-ID: 1 / Ens-ID: 1 / Beg auth comp-ID: ASP / Beg label comp-ID: ASP / End auth comp-ID: ARG / End label comp-ID: ARG / Refine code: 5 / Auth seq-ID: 3 - 367 / Label seq-ID: 3 - 367
NCS oper: (Code: given Matrix: (-0.85463, 0.17841, -0.48763), Vector: |
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Components
-Protein , 1 types, 2 molecules AB
#1: Protein | Mass: 39089.430 Da / Num. of mol.: 2 / Mutation: YES Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() |
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-Non-polymers , 5 types, 171 molecules ![](data/chem/img/MG.gif)
![](data/chem/img/PCA.gif)
![](data/chem/img/RGP.gif)
![](data/chem/img/SO4.gif)
![](data/chem/img/HOH.gif)
![](data/chem/img/PCA.gif)
![](data/chem/img/RGP.gif)
![](data/chem/img/SO4.gif)
![](data/chem/img/HOH.gif)
#2: Chemical | ChemComp-MG / | ||||||
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#3: Chemical | #4: Chemical | #5: Chemical | #6: Water | ChemComp-HOH / | |
-Details
Compound details | ENGINEERED |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.92 Å3/Da / Density % sol: 57.59 % |
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Crystal grow | pH: 6.5 / Details: 1.6 M MGSO4, 0.1 M KCL, 0.1 M MES PH 6.5 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: MARRESEARCH / Detector: CCD / Date: Oct 10, 2003 Details: A RD COATED FLAT MIRROR AND A RD COATED TOROIDAL MIRROR |
Radiation | Monochromator: SI111 DOUBLE CRYSTAL / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.979 Å / Relative weight: 1 |
Reflection | Resolution: 2.5→48.8 Å / Num. obs: 61566 / % possible obs: 99.5 % / Observed criterion σ(I): 1.7 / Redundancy: 11.1 % / Rmerge(I) obs: 0.07 / Net I/σ(I): 6.8 |
Reflection shell | Resolution: 2.5→2.64 Å / Redundancy: 6.2 % / Rmerge(I) obs: 0.42 / Mean I/σ(I) obs: 1.7 / % possible all: 99.5 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 2AKO Resolution: 2.5→88.39 Å / Cor.coef. Fo:Fc: 0.944 / Cor.coef. Fo:Fc free: 0.911 / SU B: 16.509 / SU ML: 0.183 / Cross valid method: THROUGHOUT / ESU R: 0.336 / ESU R Free: 0.252 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 37.04 Å2
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Refinement step | Cycle: LAST / Resolution: 2.5→88.39 Å
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Refine LS restraints |
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