+Open data
-Basic information
Entry | Database: PDB / ID: 1a4v | ||||||
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Title | ALPHA-LACTALBUMIN | ||||||
Components | ALPHA-LACTALBUMIN | ||||||
Keywords | LACTOSE SYNTHASE / CALCIUM BINDING / ALPHA-LACTALBUMIN | ||||||
Function / homology | Function and homology information Lactose synthesis / lactose synthase activity / lactose biosynthetic process / Golgi lumen / cell-cell signaling / lysozyme activity / defense response to bacterium / Golgi membrane / apoptotic process / calcium ion binding ...Lactose synthesis / lactose synthase activity / lactose biosynthetic process / Golgi lumen / cell-cell signaling / lysozyme activity / defense response to bacterium / Golgi membrane / apoptotic process / calcium ion binding / signal transduction / protein-containing complex / extracellular space Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / Resolution: 1.8 Å | ||||||
Authors | Chandra, N. / Acharya, K.R. | ||||||
Citation | Journal: Biochemistry / Year: 1998 Title: Structural evidence for the presence of a secondary calcium binding site in human alpha-lactalbumin. Authors: Chandra, N. / Brew, K. / Acharya, K.R. #1: Journal: Structure / Year: 1996 Title: Crystal Structures of Guinea-Pig, Goat and Bovine Alpha-Lactalbumin Highlight the Enhanced Conformational Flexibility of Regions that are Significant for its Action in Lactose Synthase Authors: Pike, A.C. / Brew, K. / Acharya, K.R. #2: Journal: J.Biol.Chem. / Year: 1994 Title: Study by Mutagenesis of the Roles of Two Aromatic Clusters of Alpha-Lactalbumin in Aspects of its Action in the Lactose Synthase System Authors: Grobler, J.A. / Wang, M. / Pike, A.C. / Brew, K. #3: Journal: J.Biol.Chem. / Year: 1993 Title: Alpha-Lactalbumin Possesses a Distinct Zinc Binding Site Authors: Ren, J. / Stuart, D.I. / Acharya, K.R. #4: Journal: J.Mol.Biol. / Year: 1991 Title: Crystal Structure of Human Alpha-Lactalbumin at 1.7 A Resolution Authors: Acharya, K.R. / Ren, J.S. / Stuart, D.I. / Phillips, D.C. / Fenna, R.E. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1a4v.cif.gz | 36.2 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1a4v.ent.gz | 27.7 KB | Display | PDB format |
PDBx/mmJSON format | 1a4v.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/a4/1a4v ftp://data.pdbj.org/pub/pdb/validation_reports/a4/1a4v | HTTPS FTP |
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-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 14093.128 Da / Num. of mol.: 1 / Fragment: CALCIUM-BINDING REGION / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) Cellular location: TRANS-GOLGI APPARATUS OF THE MAMMARY GLAND Secretion: MILK / References: UniProt: P00709, lactose synthase | ||
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#2: Chemical | #3: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 1.99 Å3/Da / Density % sol: 38 % | ||||||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | pH: 7.5 / Details: pH 7.5 | ||||||||||||||||||||||||||||||||||||||||||||||||
Crystal | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Method: vapor diffusion, hanging drop | ||||||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 293 K |
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Diffraction source | Source: ROTATING ANODE / Type: SIEMENS / Wavelength: 1.5418 |
Detector | Type: SIEMENS / Detector: AREA DETECTOR / Date: Jan 1, 1992 / Details: COLLIMATOR |
Radiation | Monochromator: GRAPHITE(002) / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 1.8→8 Å / Num. obs: 9928 / % possible obs: 82 % / Observed criterion σ(I): -3 / Redundancy: 4.1 % / Biso Wilson estimate: 5.6 Å2 / Rsym value: 0.0699 / Net I/σ(I): 14.33 |
Reflection shell | Resolution: 1.8→1.9 Å / Redundancy: 0.31 % / Mean I/σ(I) obs: 1.03 / Rsym value: 0.337 / % possible all: 64 |
Reflection | *PLUS Num. measured all: 40180 / Rmerge(I) obs: 0.0699 |
Reflection shell | *PLUS % possible obs: 64 % / Rmerge(I) obs: 0.018 |
-Processing
Software |
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Refinement | Resolution: 1.8→8 Å / Rfactor Rfree error: 0.012 / Data cutoff high absF: 10000000 / Data cutoff low absF: 0.001 / Isotropic thermal model: ISOTROPIC / Cross valid method: THROUGHOUT / σ(F): 2
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Displacement parameters | Biso mean: 16.8 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 1.8→8 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 1.8→1.86 Å / Rfactor Rfree error: 0.067 / Total num. of bins used: 10
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Xplor file |
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Software | *PLUS Name: X-PLOR / Version: 3.1 / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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