+Open data
-Basic information
Entry | Database: PDB / ID: 1h72 | |||||||||
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Title | CRYSTAL STRUCTURE OF HOMOSERINE KINASE COMPLEXED WITH HSE | |||||||||
Components | HOMOSERINE KINASE | |||||||||
Keywords | TRANSFERASE / KINASE / THREONINE BIOSYNTHESIS | |||||||||
Function / homology | Function and homology information homoserine kinase / homoserine kinase activity / threonine biosynthetic process / phosphorylation / ATP binding / cytoplasm Similarity search - Function | |||||||||
Biological species | METHANOCOCCUS JANNASCHII (archaea) | |||||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.8 Å | |||||||||
Authors | Krishna, S.S. / Zhou, T. / Daugherty, M. / Osterman, A.L. / Zhang, H. | |||||||||
Citation | Journal: Biochemistry / Year: 2001 Title: Structural Basis for the Catalysis and Substrate Specificity of Homoserine Kinase Authors: Krishna, S.S. / Zhou, T. / Daugherty, M. / Osterman, A.L. / Zhang, H. #1: Journal: Structure / Year: 2000 Title: Structure and Mechanism of Homoserine Kinase: Prototype for the Ghmp Kinase Superfamily Authors: Zhou, T. / Daugherty, M. / Grishin, N.V. / Osterman, A.L. / Zhang, H. | |||||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1h72.cif.gz | 79.5 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1h72.ent.gz | 58.7 KB | Display | PDB format |
PDBx/mmJSON format | 1h72.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1h72_validation.pdf.gz | 749.2 KB | Display | wwPDB validaton report |
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Full document | 1h72_full_validation.pdf.gz | 753.1 KB | Display | |
Data in XML | 1h72_validation.xml.gz | 9.4 KB | Display | |
Data in CIF | 1h72_validation.cif.gz | 14.6 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/h7/1h72 ftp://data.pdbj.org/pub/pdb/validation_reports/h7/1h72 | HTTPS FTP |
-Related structure data
Related structure data | 1h73C 1h74C 1fwlS S: Starting model for refinement C: citing same article (ref.) |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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Details | THE CHAIN IN THE COMPLEX IS 1422.9TROM **2 |
-Components
#1: Protein | Mass: 32299.371 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) METHANOCOCCUS JANNASCHII (archaea) / Production host: ESCHERICHIA COLI (E. coli) / References: UniProt: Q58504, homoserine kinase |
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#2: Chemical | ChemComp-HSE / |
#3: Chemical | ChemComp-ANP / |
#4: Chemical | ChemComp-TRS / |
#5: 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: 2.98 Å3/Da / Density % sol: 58.66 % | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | pH: 8 / Details: PEG4000, SODIUM ACETATE, pH 8.00 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 100 K / pH: 7.2 / 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: SYNCHROTRON / Site: APS / Beamline: 19-BM / Wavelength: 0.9793 |
Detector | Detector: IMAGE PLATE |
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→50 Å / Num. obs: 36728 / % possible obs: 99.8 % / Observed criterion σ(I): -3 / Redundancy: 5.1 % / Rmerge(I) obs: 0.089 / Net I/σ(I): 21.1 |
Reflection | *PLUS Num. measured all: 206493 |
Reflection shell | *PLUS % possible obs: 99.9 % / Mean I/σ(I) obs: 2 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 1FWL Resolution: 1.8→50 Å / Cross valid method: FREE R-VALUE / σ(F): 0
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Displacement parameters | Biso mean: 24.99 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.8→50 Å
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Refine LS restraints |
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