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Open data
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Basic information
Entry | Database: PDB / ID: 6nx6 | ||||||
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Title | ECAII(D90T,K162T) MUTANT IN COMPLEX WITH CITRATE AT PH 5 | ||||||
![]() | L-asparaginase 2 | ||||||
![]() | HYDROLASE / inactive mutant / hydrolysis of L-asparagine | ||||||
Function / homology | ![]() asparagine catabolic process / asparaginase / asparaginase activity / outer membrane-bounded periplasmic space / protein homotetramerization / protein-containing complex / identical protein binding Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Lubkowski, J. / Wlodawer, A. | ||||||
![]() | ![]() Title: Opportunistic complexes of E. coli L-asparaginases with citrate anions. Authors: Lubkowski, J. / Chan, W. / Wlodawer, A. #1: ![]() Title: Crystal structure and allosteric regulation of the cytoplasmic Escherichia coli L-asparaginase I. Authors: Yun, M.K. / Nourse, A. / White, S.W. / Rock, C.O. / Heath, R.J. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 134 KB | Display | ![]() |
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PDB format | ![]() | 108.1 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 6nx7C ![]() 6nx8C ![]() 6nx9C ![]() 6nxaC ![]() 6nxbC ![]() 6nxcC ![]() 6nxdC 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
#1: Protein | Mass: 35544.820 Da / Num. of mol.: 2 / Mutation: D90T, K162T Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Strain: K12 / Gene: ansB, b2957, JW2924 / Plasmid: pET-22b Details (production host): ORF contains a secretion sequence, 'HHHHHH' affinity tag and sequence of doubly mutated mature EcAII Cell (production host): mesophilic bacteria / Cell line (production host): JC2 / Production host: ![]() ![]() #2: Chemical | ChemComp-ACY / | #3: Chemical | ChemComp-CIT / | #4: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.88 Å3/Da / Density % sol: 57.3 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop Details: Protein, at the concentration 15 mg/ml in 50 mM HEPES buffer pH 7 and 150 mM sodium chloride was mixed with equivolume solution of precipitant that contained, 17% (w/v) PEG3350, 0.17 M ...Details: Protein, at the concentration 15 mg/ml in 50 mM HEPES buffer pH 7 and 150 mM sodium chloride was mixed with equivolume solution of precipitant that contained, 17% (w/v) PEG3350, 0.17 M ammonium citrate pH 5.0, and 20 mM L-Asn. Resulting droplets were equilibrated against the precipitant. For the data collection, crystal was mounted in a quartz capillary PH range: 5.3-5.4 / Temp details: incubator-controlled |
-Data collection
Diffraction | Mean temperature: 298 K / Ambient temp details: room temperature / Serial crystal experiment: N | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Diffraction source | Source: ![]() | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Detector | Type: DECTRIS EIGER R 4M / Detector: PIXEL / Date: Jun 10, 2018 / Details: Multilayer X-ray mirrors VariMax HF | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Radiation | Monochromator: Multilayer X-ray mirrors VariMax HF / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Reflection | Resolution: 2.15→40 Å / Num. obs: 43555 / % possible obs: 97.1 % / Redundancy: 4.1 % / Rmerge(I) obs: 0.108 / Rpim(I) all: 0.059 / Rrim(I) all: 0.125 / Χ2: 0.848 / Net I/σ(I): 8.8 / Num. measured all: 180060 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Reflection shell | Diffraction-ID: 1
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Processing
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Refinement | Method to determine structure: ![]() Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS U VALUES : REFINED INDIVIDUALLY
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso max: 132.3 Å2 / Biso mean: 31.595 Å2 / Biso min: 7.8 Å2
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Refinement step | Cycle: final / Resolution: 2.15→40 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.15→2.206 Å / Rfactor Rfree error: 0 / Total num. of bins used: 20
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