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- PDB-2gsa: CRYSTAL STRUCTURE OF GLUTAMATE-1-SEMIALDEHYDE AMINOMUTASE (AMINOT... -
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Open data
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Basic information
Entry | Database: PDB / ID: 2gsa | ||||||
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Title | CRYSTAL STRUCTURE OF GLUTAMATE-1-SEMIALDEHYDE AMINOMUTASE (AMINOTRANSFERASE, WILD-TYPE FORM) | ||||||
![]() | GLUTAMATE SEMIALDEHYDE AMINOTRANSFERASE | ||||||
![]() | CHLOROPHYLL BIOSYNTHESIS / PYRIDOXAL-5'-PHOSPHATE / PYRIDOXAMINE-5'-PHOSPHATE / ASYMMETRIC DIMER | ||||||
Function / homology | ![]() glutamate-1-semialdehyde 2,1-aminomutase / glutamate-1-semialdehyde 2,1-aminomutase activity / chlorophyll biosynthetic process / protoporphyrinogen IX biosynthetic process / transaminase activity / pyridoxal phosphate binding / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Hennig, M. / Jansonius, J.N. | ||||||
![]() | ![]() Title: Crystal structure of glutamate-1-semialdehyde aminomutase: an alpha2-dimeric vitamin B6-dependent enzyme with asymmetry in structure and active site reactivity. Authors: Hennig, M. / Grimm, B. / Contestabile, R. / John, R.A. / Jansonius, J.N. #1: ![]() Title: Crystallization and Preliminary X-Ray Analysis of Wild-Type and K272A Mutant Glutamate 1-Semialdehyde Aminotransferase from Synechococcus Authors: Hennig, M. / Grimm, B. / Jenny, M. / Muller, R. / Jansonius, J.N. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 178.1 KB | Display | ![]() |
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PDB format | ![]() | 140.4 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 412.2 KB | Display | ![]() |
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Full document | ![]() | 427.1 KB | Display | |
Data in XML | ![]() | 19.4 KB | Display | |
Data in CIF | ![]() | 31 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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1 |
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Unit cell |
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Details | THE ASYMMETRIC UNIT CONTAINS A STRUCTURALLY ASYMMETRIC HOMODIMER. |
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Components
#1: Protein | Mass: 46059.523 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() References: UniProt: P24630, glutamate-1-semialdehyde 2,1-aminomutase #2: Chemical | ChemComp-PMP / | #3: Chemical | ChemComp-PLP / | #4: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.4 Å3/Da / Density % sol: 50 % | |||||||||||||||||||||||||||||||||||
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Crystal grow | pH: 7 Details: 50MM NA-CACODYLATE BUFFER PH 7.0, 200 MM MG-ACETATE, 19.5% PEG 10,000 | |||||||||||||||||||||||||||||||||||
Crystal | *PLUS | |||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 4 ℃ / Method: vapor diffusion, sitting drop / Details: Hennig, M., (1994) J.Mol.Biol., 242, 591. | |||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 273 K |
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Diffraction source | Source: ![]() |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Mar 12, 1995 |
Radiation | Monochromator: GRAPHITE(002) / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2.4→15 Å / Num. obs: 34132 / % possible obs: 94.6 % / Redundancy: 3.25 % / Biso Wilson estimate: 32 Å2 / Rsym value: 0.068 / Net I/σ(I): 10 |
Reflection shell | Resolution: 2.4→2.52 Å / Redundancy: 2.9 % / Mean I/σ(I) obs: 2.6 / Rsym value: 0.3 / % possible all: 92.2 |
Reflection | *PLUS Num. measured all: 110780 / Rmerge(I) obs: 0.068 |
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Processing
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Refinement | Method to determine structure: ![]() Details: RESIDUES FROM HIS 153 TO THR 181 ARE DISORDERED AND HAVE OCCUPANCY 0.0.
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Displacement parameters | Biso mean: 29.6 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.4→10 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.4→2.51 Å / Total num. of bins used: 10
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Software | *PLUS Name: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Rfactor Rfree: 0.25 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS |