+Open data
-Basic information
Entry | Database: PDB / ID: 2q7m | ||||||
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Title | Crystal structure of human FLAP with MK-591 | ||||||
Components | Arachidonate 5-lipoxygenase-activating protein | ||||||
Keywords | MEMBRANE PROTEIN / LIPID TRANSPORT / MAPEG / FLAP | ||||||
Function / homology | Function and homology information leukotriene production involved in inflammatory response / arachidonate 5-lipoxygenase activity / leukotriene-C4 synthase activity / Synthesis of Lipoxins (LX) / Synthesis of 5-eicosatetraenoic acids / lipoxygenase pathway / Synthesis of Leukotrienes (LT) and Eoxins (EX) / positive regulation of acute inflammatory response / leukotriene biosynthetic process / glutathione peroxidase activity ...leukotriene production involved in inflammatory response / arachidonate 5-lipoxygenase activity / leukotriene-C4 synthase activity / Synthesis of Lipoxins (LX) / Synthesis of 5-eicosatetraenoic acids / lipoxygenase pathway / Synthesis of Leukotrienes (LT) and Eoxins (EX) / positive regulation of acute inflammatory response / leukotriene biosynthetic process / glutathione peroxidase activity / arachidonic acid binding / protein homotrimerization / glutathione transferase activity / enzyme activator activity / cellular response to calcium ion / nuclear envelope / nuclear membrane / protein-containing complex binding / endoplasmic reticulum membrane / enzyme binding / endoplasmic reticulum / membrane / identical protein binding Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 4.25 Å | ||||||
Authors | Ferguson, A.D. | ||||||
Citation | Journal: Science / Year: 2007 Title: Crystal structure of inhibitor-bound human 5-lipoxygenase-activating protein. Authors: Ferguson, A.D. / McKeever, B.M. / Xu, S. / Wisniewski, D. / Miller, D.K. / Yamin, T.T. / Spencer, R.H. / Chu, L. / Ujjainwalla, F. / Cunningham, B.R. / Evans, J.F. / Becker, J.W. | ||||||
History |
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Remark 650 | HELIX DETERMINATION METHOD: AUTHOR DETERMINED |
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2q7m.cif.gz | 185.4 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2q7m.ent.gz | 151.9 KB | Display | PDB format |
PDBx/mmJSON format | 2q7m.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/q7/2q7m ftp://data.pdbj.org/pub/pdb/validation_reports/q7/2q7m | HTTPS FTP |
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-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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2 |
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Unit cell |
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Details | The biological unit is a trimer |
-Components
#1: Protein | Mass: 18111.910 Da / Num. of mol.: 6 / Mutation: K148A Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: ALOX5AP, FLAP / Plasmid: pET28a / Species (production host): Escherichia coli / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(DE3) / References: UniProt: P20292 #2: Chemical | ChemComp-2CS / |
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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: 5.272281 Å3/Da / Density % sol: 76.670441 % |
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Crystal grow | Temperature: 298 K / Method: vapor diffusion, sitting drop / pH: 5.6 Details: 10% PEG4000, 0.32 LiCl2, 1mM TCEP , pH 5.6, VAPOR DIFFUSION, SITTING DROP, temperature 298K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: APS / Beamline: 17-ID / Wavelength: 1 Å |
Detector | Type: ADSC QUANTUM 315 / Detector: CCD / Date: Jun 1, 2006 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 4.25→38.8 Å / Num. obs: 16875 / % possible obs: 99.1 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 9.6 % / Biso Wilson estimate: 164.45 Å2 / Rmerge(I) obs: 0.058 / Net I/σ(I): 22.7 |
Reflection shell | Resolution: 4.25→4.51 Å / Redundancy: 9.6 % / Rmerge(I) obs: 0.555 / Mean I/σ(I) obs: 4.57 / % possible all: 99.1 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT / Resolution: 4.25→20 Å / Cross valid method: THROUGHOUT / σ(F): 0 / Stereochemistry target values: Engh & Huber
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Displacement parameters | Biso mean: 191.78 Å2
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Refinement step | Cycle: LAST / Resolution: 4.25→20 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 4.25→4.51 Å / Total num. of bins used: 9
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