+Open data
-Basic information
Entry | Database: PDB / ID: 1b8g | ||||||
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Title | 1-AMINOCYCLOPROPANE-1-CARBOXYLATE SYNTHASE | ||||||
Components | PROTEIN (1-AMINOCYCLOPROPANE-1-CARBOXYLATE SYNTHASE) | ||||||
Keywords | LYASE / ETHYLENE BIOSYNTHESIS | ||||||
Function / homology | Function and homology information Oxidoreductases; Acting on the CH-NH2 group of donors / 1-aminocyclopropane-1-carboxylate synthase / fruit ripening / 1-aminocyclopropane-1-carboxylate synthase activity / ethylene biosynthetic process / transaminase activity / pyridoxal phosphate binding / oxidoreductase activity Similarity search - Function | ||||||
Biological species | Malus x domestica (apple) | ||||||
Method | X-RAY DIFFRACTION / MIR / Resolution: 2.37 Å | ||||||
Authors | Capitani, G. / Hohenester, E. / Feng, L. / Storici, P. / Kirsch, J.F. / Jansonius, J.N. | ||||||
Citation | Journal: J.Mol.Biol. / Year: 1999 Title: Structure of 1-aminocyclopropane-1-carboxylate synthase, a key enzyme in the biosynthesis of the plant hormone ethylene. Authors: Capitani, G. / Hohenester, E. / Feng, L. / Storici, P. / Kirsch, J.F. / Jansonius, J.N. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1b8g.cif.gz | 179.6 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1b8g.ent.gz | 143 KB | Display | PDB format |
PDBx/mmJSON format | 1b8g.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1b8g_validation.pdf.gz | 453.7 KB | Display | wwPDB validaton report |
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Full document | 1b8g_full_validation.pdf.gz | 477.1 KB | Display | |
Data in XML | 1b8g_validation.xml.gz | 34.5 KB | Display | |
Data in CIF | 1b8g_validation.cif.gz | 47.9 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/b8/1b8g ftp://data.pdbj.org/pub/pdb/validation_reports/b8/1b8g | HTTPS FTP |
-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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Noncrystallographic symmetry (NCS) | NCS oper: (Code: given Matrix: (-0.81007, 0.57723, -0.10289), Vector: |
-Components
#1: Protein | Mass: 48263.836 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Malus x domestica (apple) / Tissue: FRUIT CORTICAL TISSUE / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3) PLYSS References: UniProt: P37821, 1-aminocyclopropane-1-carboxylate synthase #2: Chemical | #3: Water | ChemComp-HOH / | Sequence details | RESIDUE 101 TAKEN AS E (SEE CONFLICT FIELD) | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.4 Å3/Da / Density % sol: 46 % | ||||||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | pH: 7.5 / Details: pH 7.5 | ||||||||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Method: vapor diffusion, hanging dropDetails: drop consists of equal volume of protein and reservoir solutions | ||||||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 277 K |
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Diffraction source | Source: ROTATING ANODE / Type: ELLIOTT GX-20 / Wavelength: 1.5418 |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Mar 15, 1995 |
Radiation | Monochromator: GRAPHITE / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2.37→19.7 Å / Num. all: 34176 / Num. obs: 34176 / % possible obs: 93.6 % / Observed criterion σ(I): 0 / Redundancy: 1.9 % / Biso Wilson estimate: 32.3 Å2 / Rsym value: 4.7 / Net I/σ(I): 9.8 |
Reflection shell | Resolution: 2.37→2.43 Å / Redundancy: 1.7 % / Mean I/σ(I) obs: 6.2 / Rsym value: 10.4 / % possible all: 80.8 |
Reflection | *PLUS Rmerge(I) obs: 0.098 |
Reflection shell | *PLUS % possible obs: 80.8 % / Rmerge(I) obs: 0.104 |
-Processing
Software |
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Refinement | Method to determine structure: MIR / Resolution: 2.37→19.7 Å / Data cutoff high absF: 1000000 / Data cutoff low absF: 0.001 / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(F): 0 Details: THE BETA ANGLE OF THE UNIT CELL IS VERY CLOSE TO 90 DEGREES. THE SPACEGROUP HAS BEEN CAREFULLY CHECKED AND CONFIRMED AS P21
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Displacement parameters | Biso mean: 31.4 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 2.37→19.7 Å
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Refine LS restraints |
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Refine LS restraints NCS | NCS model details: RESTRAINTS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
LS refinement shell | Resolution: 2.37→2.48 Å / Total num. of bins used: 8
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Xplor file |
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Software | *PLUS Name: X-PLOR / Version: 3.851 / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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