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- PDB-4p1c: CRYSTAL STRUCTURE OF THE TOLUENE 4-MONOOXYGENASE HYDROXYLASE-FERR... -
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Open data
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Basic information
Entry | Database: PDB / ID: 4p1c | |||||||||
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Title | CRYSTAL STRUCTURE OF THE TOLUENE 4-MONOOXYGENASE HYDROXYLASE-FERREDOXIN C7S, C84A, C85A VARIANT ELECTRON-TRANSFER COMPLEX | |||||||||
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![]() | OXIDOREDUCTASE / ELECTRON-TRANSFER COMPLEX / DIIRON ENZYME COMPLEX / IRON-SULFUR / REDUCTION / HYDROXYLASE FERREDOXIN / OXYGENASE | |||||||||
Function / homology | ![]() toluene 4-monooxygenase / toluene 4-monooxygenase activity / toluene catabolic process / 2 iron, 2 sulfur cluster binding / metal ion binding Similarity search - Function | |||||||||
Biological species | ![]() | |||||||||
Method | ![]() ![]() ![]() | |||||||||
![]() | Acheson, J.F. / Fox, B.G. | |||||||||
Funding support | ![]()
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![]() | ![]() Title: Structural basis for biomolecular recognition in overlapping binding sites in a diiron enzyme system. Authors: Acheson, J.F. / Bailey, L.J. / Elsen, N.L. / Fox, B.G. | |||||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 419.4 KB | Display | ![]() |
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PDB format | ![]() | 337.8 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 4p1bC ![]() 3dhgS S: Starting model for refinement C: citing same article ( |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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Unit cell |
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Components
-Toluene-4-monooxygenase system protein ... , 3 types, 6 molecules ADBECF
#1: Protein | Mass: 57089.910 Da / Num. of mol.: 2 / Mutation: Stop>492 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() References: UniProt: Q00456, Oxidoreductases; Acting on paired donors, with incorporation or reduction of molecular oxygen; With NADH or NADPH as one donor, and incorporation of one atom of oxygen into the other donor #2: Protein | Mass: 35930.363 Da / Num. of mol.: 2 / Mutation: STOP>307 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() References: UniProt: Q00460, Oxidoreductases; Acting on paired donors, with incorporation or reduction of molecular oxygen; With NADH or NADPH as one donor, and incorporation of one atom of oxygen into the other donor #3: Protein | Mass: 9340.679 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() References: UniProt: Q00457, Oxidoreductases; Acting on paired donors, with incorporation or reduction of molecular oxygen; With NADH or NADPH as one donor, and incorporation of one atom of oxygen into the other donor |
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-Protein , 1 types, 2 molecules HI
#4: Protein | Mass: 12125.305 Da / Num. of mol.: 2 / Mutation: C7S C84A C85A Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
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-Non-polymers , 4 types, 617 molecules ![](data/chem/img/FE.gif)
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![](data/chem/img/FES.gif)
![](data/chem/img/HOH.gif)
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![](data/chem/img/FES.gif)
![](data/chem/img/HOH.gif)
#5: Chemical | ChemComp-FE / #6: Chemical | #7: Chemical | #8: Water | ChemComp-HOH / | |
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-Details
Sequence details | W336 AND Y227 ARE THE RESIDUES IN STRUCTURE. THERE MAY BE ERRORS IN THE ORIGINAL SEQUENCING OF THE ...W336 AND Y227 ARE THE RESIDUES IN STRUCTURE. THERE MAY BE ERRORS IN THE ORIGINAL SEQUENCING |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.36 Å3/Da / Density % sol: 47.88 % |
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Crystal grow | Temperature: 292 K / Method: vapor diffusion, hanging drop / pH: 7.5 Details: 100 MM MOPS/HEPES, 20% PEG 3350, 5% JEFFAMINE 200 MM AMMONIUM CHLORIDE, 10 MM MGCL2, PH 7.5, VAPOR DIFFUSION, TEMPERATURE 292K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: MARMOSAIC 300 mm CCD / Detector: CCD / Date: Nov 22, 2011 |
Radiation | Monochromator: C(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.97857 Å / Relative weight: 1 |
Reflection | Resolution: 2.4→47.69 Å / Num. obs: 81284 / % possible obs: 94.6 % / Observed criterion σ(I): 1.7 / Redundancy: 6 % / Biso Wilson estimate: 27.96 Å2 / Rsym value: 0.129 / Net I/σ(I): 12.4 |
Reflection shell | Resolution: 2.4→2.43 Å / Redundancy: 4.5 % / Mean I/σ(I) obs: 2 / Rsym value: 0.76 / % possible all: 93 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 3DHG Resolution: 2.4→47.69 Å / SU ML: 0.27 / Cross valid method: FREE R-VALUE / σ(F): 1.34 / Phase error: 21.24 / Stereochemistry target values: ML
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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: 20.16 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.4→47.69 Å
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Refine LS restraints |
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LS refinement shell |
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