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Open data
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Basic information
Entry | Database: PDB / ID: 1fkv | ||||||
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Title | RECOMBINANT GOAT ALPHA-LACTALBUMIN T29I | ||||||
![]() | ALPHA-LACTALBUMIN | ||||||
![]() | TRANSFERASE / LACTOSE SYNTHASE COMPONENT / CALCIUM BINDING METALLOPROTEIN / GLYCOPROTEIN | ||||||
Function / homology | ![]() lactose synthase activity / lactose biosynthetic process / lysozyme activity / defense response to Gram-negative bacterium / defense response to Gram-positive bacterium / calcium ion binding / protein-containing complex / extracellular region Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() | ||||||
![]() | Horii, K. / Matsushima, M. / Tsumoto, K. / Kumagai, I. | ||||||
![]() | ![]() Title: Contribution of Thr29 to the thermodynamic stability of goat alpha-lactalbumin as determined by experimental and theoretical approaches. Authors: Horii, K. / Saito, M. / Yoda, T. / Tsumoto, K. / Matsushima, M. / Kuwajima, K. / Kumagai, I. #1: ![]() Title: Effect of the extra N-terminal Methionine residue on the stability and folding of recombinant alpha-lactalbumin expressed in Escherichia coli Authors: Chaudhuri, T.K. / Horii, K. / Yoda, T. / Arai, M. / Nagata, S. / Terada, T.P. / Uchiyama, H. / Ikura, T. / Tsumoto, K. / Kataoka, H. / Matsushima, M. / Kuwajima, K. / Kumagai, I. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 34.8 KB | Display | ![]() |
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PDB format | ![]() | 25.7 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 365.4 KB | Display | ![]() |
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Full document | ![]() | 365.8 KB | Display | |
Data in XML | ![]() | 3.7 KB | Display | |
Data in CIF | ![]() | 5.5 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related 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: 14354.307 Da / Num. of mol.: 1 / Fragment: B-HELIX / Mutation: YES Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() |
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#2: Chemical | ChemComp-CA / |
#3: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.24 Å3/Da / Density % sol: 45.13 % | |||||||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 6 Details: PEG 8000, calcium chloride, potassium phosphate, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K | |||||||||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 4 ℃ | |||||||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 282.5 K |
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Diffraction source | Source: ![]() |
Detector | Type: MACSCIENCE / Detector: IMAGE PLATE / Date: Sep 5, 1997 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2→30 Å / Num. all: 9147 / Num. obs: 8712 / % possible obs: 95.3 % / Redundancy: 4.7 % / Rmerge(I) obs: 0.089 / Net I/σ(I): 8.4 |
Reflection shell | Resolution: 2→2.07 Å / Rmerge(I) obs: 0.218 / % possible all: 95.6 |
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Processing
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Refinement | Resolution: 2→8 Å / σ(F): 2 / Stereochemistry target values: Engh & Huber Details: The C-terminal tripeptide (Glu121-Leu123) is poorly defined in the electron density and therefore these residues have not been included in the final model.
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Refinement step | Cycle: LAST / Resolution: 2→8 Å
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Refine LS restraints |
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Refinement | *PLUS % reflection Rfree: 10 % / Rfactor obs: 0.193 | |||||||||||||||||||||||||
Solvent computation | *PLUS | |||||||||||||||||||||||||
Displacement parameters | *PLUS |