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- PDB-2uyt: Structure of L-rhamnulose kinase in complex with ADP and beta-L- ... -
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Open data
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Basic information
Entry | Database: PDB / ID: 2uyt | ||||||
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Title | Structure of L-rhamnulose kinase in complex with ADP and beta-L- rhamnulose. | ||||||
![]() | RHAMNULOKINASE | ||||||
![]() | TRANSFERASE / RHAMNOSE DEGRADATION / IN-LINE PHOSPHORYL TRANSFER / HEXOKINASE-HSP70-ACTIN SUPERFAMILY / L-RHAMNULOSE KINASE / RHAMNOSE METABOLISM / KINASE / INDUCED FIT / RARE SUGARS | ||||||
Function / homology | ![]() rhamnulokinase / rhamnulokinase activity / rhamnose catabolic process / glycerol kinase activity / glycerol metabolic process / ATP binding / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Grueninger, D. / Schulz, G.E. | ||||||
![]() | ![]() Title: Substrate Spectrum of L-Rhamnulose Kinase Related to Models Derived from Two Ternary Complex Structures. Authors: Grueninger, D. / Schulz, G.E. #1: ![]() Title: Structure and Reaction Mechanism of L-Rhamnulose Kinase from Escherichia Coli Authors: Grueninger, D. / Schulz, G.E. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 116.2 KB | Display | ![]() |
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PDB format | ![]() | 87.6 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 777.8 KB | Display | ![]() |
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Full document | ![]() | 781.1 KB | Display | |
Data in XML | ![]() | 21.6 KB | Display | |
Data in CIF | ![]() | 32.6 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 2cglS 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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Components
#1: Protein | Mass: 53954.715 Da / Num. of mol.: 1 / Mutation: YES Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() References: UniProt: Q8X899, UniProt: Q1R415*PLUS, rhamnulokinase |
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#2: Sugar | ChemComp-LRH / |
#3: Chemical | ChemComp-ADP / |
#4: Water | ChemComp-HOH / |
Compound details | ENGINEERED RESIDUE IN CHAIN A, GLU 69 TO ALA ENGINEERED RESIDUE IN CHAIN A, GLU 70 TO ALA ...ENGINEERED |
Sequence details | THE SEQUENCE DISCREPANCIES ARE BECAUSE THE DATABASE SEQUENCE IS FROM E.COLI STRAIN O157-H7. THE ...THE SEQUENCE DISCREPANC |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 1.9 Å3/Da / Density % sol: 35 % |
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Crystal grow | Details: 17% (W/V) PEG 8000, 0.12 M LICL, 20 MM ADP, 20 MM L-RHAMNULOSE-1-PHOSPHATE |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: MARRESEARCH / Detector: CCD |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.91841 Å / Relative weight: 1 |
Reflection | Resolution: 1.55→80 Å / Num. obs: 60401 / % possible obs: 98.6 % / Observed criterion σ(I): 4.7 / Redundancy: 6.9 % / Rmerge(I) obs: 0.05 / Net I/σ(I): 23.2 |
Reflection shell | Resolution: 1.55→1.62 Å / Redundancy: 5.5 % / Rmerge(I) obs: 0.37 / Mean I/σ(I) obs: 4.7 / % possible all: 89.4 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 2CGL Resolution: 1.55→79.31 Å / Cor.coef. Fo:Fc: 0.959 / Cor.coef. Fo:Fc free: 0.944 / SU B: 3.162 / SU ML: 0.061 / TLS residual ADP flag: LIKELY RESIDUAL / Cross valid method: THROUGHOUT / ESU R: 0.091 / ESU R Free: 0.089 / 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: 1.4 Å / Solvent model: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 14.5 Å2
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Refinement step | Cycle: LAST / Resolution: 1.55→79.31 Å
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Refine LS restraints |
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