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Open data
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Basic information
Entry | Database: PDB / ID: 1e2a | ||||||
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Title | ENZYME IIA FROM THE LACTOSE SPECIFIC PTS FROM LACTOCOCCUS LACTIS | ||||||
![]() | ENZYME IIA | ||||||
![]() | TRANSFERASE / ENZYME IIA / HELICAL BUNDLES / PTS / PHOSPHOTRANSFERASE SYSTEM | ||||||
Function / homology | ![]() phosphoenolpyruvate-dependent sugar phosphotransferase system / transferase activity / metal ion binding / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Sliz, P. / Engelmann, R. / Hengstenberg, W. / Pai, E.F. | ||||||
![]() | ![]() Title: The structure of enzyme IIAlactose from Lactococcus lactis reveals a new fold and points to possible interactions of a multicomponent system. Authors: Sliz, P. / Engelmann, R. / Hengstenberg, W. / Pai, E.F. #1: ![]() Title: Crystallization and Preliminary Structural Studies of Lactose-Specific Enzyme Iia from Lactococcus Lactis Authors: Sliz, P. / Schorter, K.H. / De Vos, W.M. / Pai, E.F. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 69.7 KB | Display | ![]() |
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PDB format | ![]() | 52.9 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 374.2 KB | Display | ![]() |
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Full document | ![]() | 375.8 KB | Display | |
Data in XML | ![]() | 6.7 KB | Display | |
Data in CIF | ![]() | 10.4 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
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 oper:
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Components
#1: Protein | Mass: 11463.118 Da / Num. of mol.: 3 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Strain: MG1820 / Gene: LACF / Production host: ![]() ![]() References: UniProt: P23532, protein-Npi-phosphohistidine-sugar phosphotransferase #2: Chemical | ChemComp-MG / | #3: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.48 Å3/Da / Density % sol: 48 % | ||||||||||||||||||||
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Crystal grow | Method: vapor diffusion, sitting drop / pH: 6.4 Details: CRYSTALS WERE OBTAINED BY THE SITTING-DROP VAPOR-DIFFUSION TECHNIQUE AT ROOM TEMPERATURE USING A SMALL INCREASE IN THE PHOSPHATE BUFFER. THE PROTEIN SOLUTION WAS MIXED WITH 0.15M NA/K ...Details: CRYSTALS WERE OBTAINED BY THE SITTING-DROP VAPOR-DIFFUSION TECHNIQUE AT ROOM TEMPERATURE USING A SMALL INCREASE IN THE PHOSPHATE BUFFER. THE PROTEIN SOLUTION WAS MIXED WITH 0.15M NA/K PHOSPHATE BUFFER, PH 6.4. THE LARGEST CRYSTALS APPEARED IN CIRCA A WEEK., vapor diffusion - sitting drop Temp details: room temp | ||||||||||||||||||||
Crystal | *PLUS | ||||||||||||||||||||
Crystal grow | *PLUS Temperature: 25 ℃ / Method: vapor diffusion, sitting drop | ||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 298 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Oct 1, 1995 |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.94 Å / Relative weight: 1 |
Reflection | Resolution: 2.3→15 Å / Num. obs: 16632 / % possible obs: 97.7 % / Observed criterion σ(I): 0 / Redundancy: 6.1 % / Rsym value: 0.086 / Net I/σ(I): 18.3 |
Reflection shell | Resolution: 2.3→2.4 Å / Redundancy: 4.9 % / Mean I/σ(I) obs: 4.9 / Rsym value: 0.36 / % possible all: 98.9 |
Reflection | *PLUS Rmerge(I) obs: 0.086 |
Reflection shell | *PLUS % possible obs: 98.9 % / Rmerge(I) obs: 0.363 |
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Processing
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Refinement | Method to determine structure: SINGLE ISOMORPHOUS REPLACEMENT, ANOMALOUS SCATTERING (SIRAS) Resolution: 2.3→8 Å / Data cutoff low absF: 0 / Cross valid method: THROUGHOUT / σ(F): 0
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Displacement parameters | Biso mean: 35 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.3→8 Å
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Software | *PLUS Name: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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