+Open data
-Basic information
Entry | Database: PDB / ID: 1hs6 | ||||||
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Title | STRUCTURE OF LEUKOTRIENE A4 HYDROLASE COMPLEXED WITH BESTATIN. | ||||||
Components | LEUKOTRIENE A-4 HYDROLASE | ||||||
Keywords | HYDROLASE / protein-inhibitor complex / alpha-beta protein | ||||||
Function / homology | Function and homology information leukotriene-A4 hydrolase / leukotriene-A4 hydrolase activity / tripeptide aminopeptidase activity / tripeptide aminopeptidase / Biosynthesis of protectins / Biosynthesis of aspirin-triggered D-series resolvins / Biosynthesis of E-series 18(R)-resolvins / Biosynthesis of D-series resolvins / Biosynthesis of E-series 18(S)-resolvins / protein metabolic process ...leukotriene-A4 hydrolase / leukotriene-A4 hydrolase activity / tripeptide aminopeptidase activity / tripeptide aminopeptidase / Biosynthesis of protectins / Biosynthesis of aspirin-triggered D-series resolvins / Biosynthesis of E-series 18(R)-resolvins / Biosynthesis of D-series resolvins / Biosynthesis of E-series 18(S)-resolvins / protein metabolic process / Synthesis of Leukotrienes (LT) and Eoxins (EX) / epoxide hydrolase activity / leukotriene biosynthetic process / type I pneumocyte differentiation / peptide catabolic process / response to zinc ion / metalloaminopeptidase activity / aminopeptidase activity / lipid metabolic process / response to peptide hormone / tertiary granule lumen / peptidase activity / ficolin-1-rich granule lumen / Neutrophil degranulation / proteolysis / RNA binding / extracellular exosome / zinc ion binding / extracellular region / nucleoplasm / nucleus / cytosol Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MAD / Resolution: 1.95 Å | ||||||
Authors | Thunnissen, M.M.G.M. / Nordlund, P.N. / Haeggstrom, J.Z. | ||||||
Citation | Journal: Nat.Struct.Biol. / Year: 2001 Title: Crystal structure of human leukotriene A(4) hydrolase, a bifunctional enzyme in inflammation. Authors: Thunnissen, M.M. / Nordlund, P. / Haeggstrom, J.Z. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1hs6.cif.gz | 149.2 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1hs6.ent.gz | 114.4 KB | Display | PDB format |
PDBx/mmJSON format | 1hs6.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1hs6_validation.pdf.gz | 471.9 KB | Display | wwPDB validaton report |
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Full document | 1hs6_full_validation.pdf.gz | 498.2 KB | Display | |
Data in XML | 1hs6_validation.xml.gz | 16.5 KB | Display | |
Data in CIF | 1hs6_validation.cif.gz | 27.8 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/hs/1hs6 ftp://data.pdbj.org/pub/pdb/validation_reports/hs/1hs6 | 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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-Components
-Protein , 1 types, 1 molecules A
#1: Protein | Mass: 69363.969 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Plasmid: PT3-MB4 / Production host: Escherichia coli (E. coli) / References: UniProt: P09960, leukotriene-A4 hydrolase |
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-Non-polymers , 6 types, 558 molecules
#2: Chemical | ChemComp-ZN / | ||||||||
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#3: Chemical | #4: Chemical | ChemComp-ACT / | #5: Chemical | ChemComp-BES / | #6: Chemical | ChemComp-IMD / | #7: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 2 |
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-Sample preparation
Crystal | Density Matthews: 2.71 Å3/Da / Density % sol: 54.63 % | ||||||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 298 K / Method: liquid diffusion / pH: 6.8 Details: PEG8000, imidazole, sodium acetate, ytterbium chloride, bestatin, pH 6.8, LIQUID DIFFUSION, temperature 298K | ||||||||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Method: liquid-liquid diffusion | ||||||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 100 K | |||||||||||||||
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Diffraction source | Source: SYNCHROTRON / Site: ESRF / Beamline: BM14 / Wavelength: 0.992, 1.3838, 1.3842, 0.8856 | |||||||||||||||
Detector | Type: MARRESEARCH / Detector: AREA DETECTOR / Date: Jul 12, 1998 | |||||||||||||||
Radiation | Monochromator: Si(111) / Protocol: MAD / Monochromatic (M) / Laue (L): M / Scattering type: x-ray | |||||||||||||||
Radiation wavelength |
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Reflection | Resolution: 1.95→34 Å / Num. all: 54827 / Num. obs: 54827 / % possible obs: 97.7 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 4.7 % / Biso Wilson estimate: 20.906 Å2 / Rmerge(I) obs: 0.043 / Net I/σ(I): 6.59 | |||||||||||||||
Reflection shell | Resolution: 1.95→2.05 Å / Redundancy: 3.6 % / Rmerge(I) obs: 0.186 / Mean I/σ(I) obs: 3.9 / % possible all: 89.6 | |||||||||||||||
Reflection | *PLUS |
-Processing
Software |
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Refinement | Method to determine structure: MAD / Resolution: 1.95→25 Å / σ(F): 0 / σ(I): 0 / Stereochemistry target values: Engh & Huber
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Refinement step | Cycle: LAST / Resolution: 1.95→25 Å
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Refine LS restraints |
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Software | *PLUS Name: TNT / Classification: refinement | ||||||||||||||||||||
Refinement | *PLUS Lowest resolution: 25 Å / σ(F): 0 / Rfactor all: 0.185 | ||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||
Refine LS restraints | *PLUS Type: t_angle_deg / Dev ideal: 2.2 |