+Open data
-Basic information
Entry | Database: PDB / ID: 8eeg | ||||||
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Title | C. ammoniagenes monoamine oxidase (MAO) bound to dopamine | ||||||
Components | Amine oxidase | ||||||
Keywords | FLAVOPROTEIN / Monoamine / oxidase / substrate / flavoenzyme | ||||||
Function / homology | Amine oxidase / Flavin containing amine oxidoreductase / FAD/NAD(P)-binding domain superfamily / oxidoreductase activity / FLAVIN-ADENINE DINUCLEOTIDE / L-DOPAMINE / Amine oxidase Function and homology information | ||||||
Biological species | Corynebacterium ammoniagenes (bacteria) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.15 Å | ||||||
Authors | Muellers, S.N. / Allen, K.N. | ||||||
Funding support | 1items
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Citation | Journal: Biochemistry / Year: 2023 Title: Structural Insights into the Substrate Range of a Bacterial Monoamine Oxidase. Authors: Muellers, S.N. / Tararina, M.A. / Kuzmanovic, U. / Galagan, J.E. / Allen, K.N. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 8eeg.cif.gz | 190.5 KB | Display | PDBx/mmCIF format |
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PDB format | pdb8eeg.ent.gz | 147.6 KB | Display | PDB format |
PDBx/mmJSON format | 8eeg.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 8eeg_validation.pdf.gz | 1.2 MB | Display | wwPDB validaton report |
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Full document | 8eeg_full_validation.pdf.gz | 1.3 MB | Display | |
Data in XML | 8eeg_validation.xml.gz | 36.3 KB | Display | |
Data in CIF | 8eeg_validation.cif.gz | 50.4 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ee/8eeg ftp://data.pdbj.org/pub/pdb/validation_reports/ee/8eeg | HTTPS FTP |
-Related structure data
Related structure data | 8eefC 8eehC 8eeiC 8eejC 8eekC 8eelC 8eemC 8eenC 8eeoC C: citing same article (ref.) |
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Similar structure data | Similarity search - Function & homologyF&H Search |
-Links
-Assembly
Deposited unit |
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1 |
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2 |
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Unit cell |
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-Components
#1: Protein | Mass: 50022.473 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Corynebacterium ammoniagenes (bacteria) Gene: CA40472_00570 / Production host: Escherichia coli (E. coli) / References: UniProt: A0A807MR40 #2: Chemical | #3: Chemical | #4: Water | ChemComp-HOH / | Has ligand of interest | Y | |
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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: 2.26 Å3/Da / Density % sol: 45.6 % |
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Crystal grow | Temperature: 290 K / Method: vapor diffusion, hanging drop Details: 10 - 15% w/v PEG-3350, 0.1 M sodium malonate, pH 5.0 |
-Data collection
Diffraction | Mean temperature: 100 K / Serial crystal experiment: N |
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Diffraction source | Source: SYNCHROTRON / Site: NSLS-II / Beamline: 17-ID-2 / Wavelength: 0.987 Å |
Detector | Type: DECTRIS EIGER X 16M / Detector: PIXEL / Date: Mar 23, 2021 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.987 Å / Relative weight: 1 |
Reflection | Resolution: 2.15→29.96 Å / Num. obs: 49977 / % possible obs: 99.67 % / Redundancy: 13.4 % / Biso Wilson estimate: 20.67 Å2 / CC1/2: 0.997 / Rmerge(I) obs: 0.473 / Rpim(I) all: 0.133 / Rrim(I) all: 0.492 / Net I/σ(I): 16.3 |
Reflection shell | Resolution: 2.15→2.227 Å / Redundancy: 13.4 % / Rmerge(I) obs: 1.083 / Mean I/σ(I) obs: 4.3 / Num. unique obs: 4913 / CC1/2: 0.945 / Rpim(I) all: 0.305 / Rrim(I) all: 1.126 / % possible all: 99.35 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT / Resolution: 2.15→29.96 Å / SU ML: 0.2259 / Cross valid method: FREE R-VALUE / σ(F): 1.35 / Phase error: 24.8659 Stereochemistry target values: GeoStd + Monomer Library + CDL v1.2
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 22.15 Å2 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.15→29.96 Å
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Refine LS restraints |
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LS refinement shell |
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