+Open data
-Basic information
Entry | Database: PDB / ID: 1dhp | ||||||
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Title | DIHYDRODIPICOLINATE SYNTHASE | ||||||
Components | DIHYDRODIPICOLINATE SYNTHASE | ||||||
Keywords | SYNTHASE / DIHYDRODIPICOLINATE | ||||||
Function / homology | Function and homology information 4-hydroxy-tetrahydrodipicolinate synthase / 4-hydroxy-tetrahydrodipicolinate synthase activity / diaminopimelate biosynthetic process / lysine biosynthetic process via diaminopimelate / identical protein binding / cytosol Similarity search - Function | ||||||
Biological species | Escherichia coli (E. coli) | ||||||
Method | X-RAY DIFFRACTION / Resolution: 2.3 Å | ||||||
Authors | Mirwaldt, C. / Korndoerfer, I. / Huber, R. | ||||||
Citation | Journal: J.Mol.Biol. / Year: 1995 Title: The crystal structure of dihydrodipicolinate synthase from Escherichia coli at 2.5 A resolution. Authors: Mirwaldt, C. / Korndorfer, I. / Huber, R. #1: Journal: Biochem.J. / Year: 1992 Title: Escherichia Coli Dihydrodipicolinate Synthase. Identification of the Active Site and Crystallization Authors: Laber, B. / Gomis-Ruth, F.X. / Romao, M.J. / Huber, R. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1dhp.cif.gz | 125.6 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1dhp.ent.gz | 97.8 KB | Display | PDB format |
PDBx/mmJSON format | 1dhp.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1dhp_validation.pdf.gz | 374.5 KB | Display | wwPDB validaton report |
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Full document | 1dhp_full_validation.pdf.gz | 383.1 KB | Display | |
Data in XML | 1dhp_validation.xml.gz | 12.6 KB | Display | |
Data in CIF | 1dhp_validation.cif.gz | 21 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/dh/1dhp ftp://data.pdbj.org/pub/pdb/validation_reports/dh/1dhp | HTTPS FTP |
-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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2 |
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Unit cell |
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Noncrystallographic symmetry (NCS) | NCS oper: (Code: given Matrix: (-0.999991, -0.003331, 0.002795), Vector: |
-Components
#1: Protein | Mass: 31304.936 Da / Num. of mol.: 2 / Mutation: A207T Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) / Gene: DAPA / Plasmid: PDB12 / Gene (production host): DAPA / Production host: Escherichia coli (E. coli) / References: UniProt: P0A6L2, dihydrodipicolinate synthase #2: Chemical | #3: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 3.76 Å3/Da / Density % sol: 66 % | ||||||||||||||||||||||||||||||
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Crystal grow | *PLUS Temperature: 4 ℃ / Method: vapor diffusion, sitting drop / Details: Laber, B., (1992) Biochem.J., 288, 691. / PH range low: 10 / PH range high: 4 | ||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction source | Wavelength: 1.5418 |
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Detector | Type: MARRESEARCH / Detector: IMAGE PLATE |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Redundancy: 3.7 % / Rmerge(I) obs: 0.038 |
-Processing
Software |
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Refinement | Resolution: 2.3→8 Å / σ(F): 2 /
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Displacement parameters | Biso mean: 23.73 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine analyze | Luzzati coordinate error obs: 0.25 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.3→8 Å
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Refine LS restraints |
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