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- PDB-1hl2: Crystal structure of N-acetylneuraminate lyase from E. coli mutan... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1hl2 | ||||||
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Title | Crystal structure of N-acetylneuraminate lyase from E. coli mutant L142R in complex with b-hydroxypyruvate | ||||||
![]() | N-ACETYLNEURAMINATE LYASE SUBUNIT | ||||||
![]() | LYASE / N-ACETYLNEURAMINATE LYASE / CLASS I ALDOLASE / CARBOHYDRATE METABOLISM / SCHIFF BASE | ||||||
Function / homology | ![]() N-acetylneuraminate lyase / N-acetylneuraminate lyase activity / N-acetylneuraminate catabolic process / single-species biofilm formation / carbohydrate metabolic process / identical protein binding / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Joerger, A.C. / Fersht, A.R. | ||||||
![]() | ![]() Title: Mimicking Natural Evolution in Vitro: An N-Acetylneuraminate Lyase Mutant with an Increased Dihydrodipicolinate Synthase Activity Authors: Joerger, A.C. / Mayer, S. / Fersht, A.R. #1: ![]() Title: Structure and Mechanism of a Sub-Family of Enzymes Related to N-Acetylneuraminate Lyase Authors: Lawrence, M.C. / Barbosa, J.A. / Smith, B.J. / Hall, N.E. / Pilling, P.A. / Ooi, H.C. / Marcuccio, S.M. #2: ![]() Title: The Three-Dimensional Structure of N-Acetylneuraminate Lyase from Escherichia Coli Authors: Izard, T. / Lawrence, M.C. / Malby, R. / Lilley, G.G. / Colman, P.M. | ||||||
History |
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Remark 700 | SHEET DETERMINATION METHOD: DSSP THE SHEETS PRESENTED AS "AA" IN EACH CHAIN ON SHEET RECORDS BELOW ... SHEET DETERMINATION METHOD: DSSP THE SHEETS PRESENTED AS "AA" IN EACH CHAIN ON SHEET RECORDS BELOW IS ACTUALLY AN 9-STRANDED BARREL THIS IS REPRESENTED BY A 10-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS ARE IDENTICAL. THE SHEETS PRESENTED AS "BA" IN EACH CHAIN ON SHEET RECORDS BELOW IS ACTUALLY AN 9-STRANDED BARREL THIS IS REPRESENTED BY A 10-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS ARE IDENTICAL. THE SHEETS PRESENTED AS "CA" IN EACH CHAIN ON SHEET RECORDS BELOW IS ACTUALLY AN 8-STRANDED BARREL THIS IS REPRESENTED BY A 9-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS ARE IDENTICAL. THE SHEETS PRESENTED AS "DA" IN EACH CHAIN ON SHEET RECORDS BELOW IS ACTUALLY AN 7-STRANDED BARREL THIS IS REPRESENTED BY A 8-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS ARE IDENTICAL. |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 248 KB | Display | ![]() |
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PDB format | ![]() | 200.1 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 471.7 KB | Display | ![]() |
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Full document | ![]() | 490.2 KB | Display | |
Data in XML | ![]() | 52.9 KB | Display | |
Data in CIF | ![]() | 76 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1fdyS 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: 32670.410 Da / Num. of mol.: 4 / Mutation: YES Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() References: UniProt: P06995, UniProt: P0A6L4*PLUS, N-acetylneuraminate lyase #2: Chemical | ChemComp-3PY / #3: Water | ChemComp-HOH / | Compound details | CATALYSES THE CONVERION OF N-ACETYLNEURAMINATE TO N-ACETYL-D-MANNOSAMINE AND PYRUVATE. ENGINEERED ...CATALYSES THE CONVERION OF N-ACETYLNEUR | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.5 Å3/Da / Density % sol: 50.71 % | ||||||||||||||||||||||||||||||||||||
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Crystal grow | pH: 4.6 / Details: pH 4.60 | ||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 21 ℃ / pH: 7.6 / Method: vapor diffusion, hanging drop | ||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Date: Sep 15, 2002 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9793 Å / Relative weight: 1 |
Reflection | Resolution: 1.8→37.4 Å / Num. obs: 117329 / % possible obs: 98.8 % / Redundancy: 3.5 % / Rmerge(I) obs: 0.071 / Net I/σ(I): 5.2 |
Reflection shell | Resolution: 1.8→1.9 Å / Redundancy: 3.4 % / Rmerge(I) obs: 0.3 / Mean I/σ(I) obs: 2.4 / % possible all: 97.7 |
Reflection | *PLUS Num. measured all: 412908 |
Reflection shell | *PLUS % possible obs: 97.7 % / Rmerge(I) obs: 0.3 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 1FDY Resolution: 1.8→37.4 Å / Cross valid method: THROUGHOUT / σ(F): 0
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Refinement step | Cycle: LAST / Resolution: 1.8→37.4 Å
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Refine LS restraints |
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Refinement | *PLUS Rfactor Rfree: 0.21 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS |