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- PDB-2uyv: L-RHAMNULOSE-1-PHOSPHATE ALDOLASE FROM ESCHERICHIA COLI (MUTANT Q... -
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Open data
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Basic information
Entry | Database: PDB / ID: 2uyv | ||||||
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Title | L-RHAMNULOSE-1-PHOSPHATE ALDOLASE FROM ESCHERICHIA COLI (MUTANT Q6Y- E192A) | ||||||
![]() | RHAMNULOSE-1-PHOSPHATE ALDOLASE | ||||||
![]() | LYASE / AGGREGATION / ZINC ENZYME / FIBRILLATION / METAL-BINDING / OLIGOMERIZATION / INTERFACE DESIGN / SURFACE MUTATION / 2-KETOSE DEGRADATION / PROTEIN-PROTEIN INTERFACE / ZINC / ALDOLASE / CLASS II / RARE SUGAR / CLEAVAGE OF L-RHAMNULOSE-1-PHOSPHATE TO DIHYDROXYACETONEPH BACTERIAL L-RHAMNOSE METABOLISM / RHAMNOSE METABOLISM / PROTEIN ENGINEERING | ||||||
Function / homology | ![]() rhamnulose-1-phosphate aldolase / rhamnulose-1-phosphate aldolase activity / rhamnose catabolic process / pentose catabolic process / aldehyde-lyase activity / identical protein binding / metal ion binding / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Grueninger, D. / Schulz, G.E. | ||||||
![]() | ![]() Title: Designed Protein-Protein Association. Authors: Grueninger, D. / Treiber, N. / Ziegler, M.O.P. / Koetter, J.W.A. / Schulze, M.-S. / Schulz, G.E. #1: ![]() Title: Structure and Catalytic Mechanism of L-Rhamnulose-1-Phosphate Aldolase Authors: Kroemer, M. / Merkel, I. / 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 | ![]() | 242.2 KB | Display | ![]() |
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PDB format | ![]() | 196.5 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 2uyuC ![]() 2v7gC ![]() 2v9eC ![]() 2v9fC ![]() 2v9gC ![]() 2v9iC ![]() 2v9lC ![]() 2v9mC ![]() 2v9nC ![]() 2v9oC ![]() 2v9uC ![]() 1ojrS S: Starting model for refinement C: citing same article ( |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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1 | ![]()
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Unit cell |
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Components on special symmetry positions |
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Noncrystallographic symmetry (NCS) | NCS oper: (Code: given) |
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Components
#1: Protein | Mass: 30151.416 Da / Num. of mol.: 4 / Mutation: YES Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() References: UniProt: P32169, rhamnulose-1-phosphate aldolase #2: Chemical | ChemComp-TLA / #3: Chemical | ChemComp-ZN / #4: Water | ChemComp-HOH / | Compound details | ENGINEERED RESIDUE IN CHAIN A, GLN 6 TO TYR ENGINEERED RESIDUE IN CHAIN A, GLU 192 TO ALA ...ENGINEERED | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.7 Å3/Da / Density % sol: 54.4 % / Description: NONE |
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Crystal grow | pH: 7.7 / Details: 1.0 M NA/K-TARTRATE, 0.1 M HEPES (PH 7.7) |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: MARRESEARCH / Detector: CCD / Date: Oct 15, 2003 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.8123 Å / Relative weight: 1 |
Reflection | Resolution: 2.2→20 Å / Num. obs: 62025 / % possible obs: 98.6 % / Observed criterion σ(I): 3.87 / Redundancy: 4.12 % / Rmerge(I) obs: 0.06 / Net I/σ(I): 15.15 |
Reflection shell | Resolution: 2.2→2.3 Å / Redundancy: 4.04 % / Rmerge(I) obs: 0.38 / Mean I/σ(I) obs: 3.87 / % possible all: 99.7 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 1OJR Resolution: 2.2→20 Å / Data cutoff high absF: 10000 / Cross valid method: RMSD / σ(F): 0 Details: THE STRUCTURE WAS REFINED USING NCS- RESTRAINT WHICH IS DEFINED IN NCS.DEF.
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Solvent computation | Bsol: 73.3316 Å2 / ksol: 0.359376 e/Å3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 39.142 Å2
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Refinement step | Cycle: LAST / Resolution: 2.2→20 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.23→2.25 Å / Total num. of bins used: 48 /
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Xplor file |
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