+Open data
-Basic information
Entry | Database: PDB / ID: 1p57 | ||||||
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Title | Extracellular domain of human hepsin | ||||||
Components | (Serine protease hepsin) x 2 | ||||||
Keywords | HYDROLASE/HYDROLASE INHIBITOR / srcr / scavenger receptor cysteine-rich domain / serine protease / HYDROLASE-HYDROLASE INHIBITOR complex | ||||||
Function / homology | Function and homology information hepsin / pilomotor reflex / Signaling by MST1 / positive regulation of thyroid hormone generation / cochlea morphogenesis / serine-type exopeptidase activity / positive regulation of plasminogen activation / basement membrane disassembly / detection of mechanical stimulus involved in sensory perception of sound / MET Receptor Activation ...hepsin / pilomotor reflex / Signaling by MST1 / positive regulation of thyroid hormone generation / cochlea morphogenesis / serine-type exopeptidase activity / positive regulation of plasminogen activation / basement membrane disassembly / detection of mechanical stimulus involved in sensory perception of sound / MET Receptor Activation / response to thyroid hormone / negative regulation of epithelial to mesenchymal transition / positive regulation by host of viral transcription / positive regulation of hepatocyte proliferation / potassium ion transmembrane transport / serine-type peptidase activity / negative regulation of epithelial cell proliferation / cell-cell junction / peptidase activity / regulation of cell shape / positive regulation of cell growth / apical plasma membrane / serine-type endopeptidase activity / neuronal cell body / positive regulation of gene expression / endoplasmic reticulum membrane / negative regulation of apoptotic process / cell surface / proteolysis / extracellular exosome / membrane / plasma membrane Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution: 1.75 Å | ||||||
Authors | Somoza, J.R. / Ho, J.D. / Luong, C. / Sprengeler, P.A. / Mortara, K. / Shrader, W.D. / Sperandio, D. / Chan, H. / McGrath, M.E. / Katz, B.A. | ||||||
Citation | Journal: Structure / Year: 2003 Title: The Structure of the Extracellular Region of Human Hepsin Reveals a Serine Protease Domain and a Novel Scavenger Receptor Cysteine-Rich (SRCR) Domain Authors: Somoza, J.R. / Ho, J.D. / Luong, C. / Ghate, M. / Sprengeler, P.A. / Mortara, K. / Shrader, W.D. / Sperandio, D. / Chan, H. / McGrath, M.E. / Katz, B.A. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1p57.cif.gz | 163.4 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1p57.ent.gz | 129.4 KB | Display | PDB format |
PDBx/mmJSON format | 1p57.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1p57_validation.pdf.gz | 678.9 KB | Display | wwPDB validaton report |
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Full document | 1p57_full_validation.pdf.gz | 690.1 KB | Display | |
Data in XML | 1p57_validation.xml.gz | 19.7 KB | Display | |
Data in CIF | 1p57_validation.cif.gz | 28.4 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/p5/1p57 ftp://data.pdbj.org/pub/pdb/validation_reports/p5/1p57 | HTTPS FTP |
-Related structure data
Related structure data | 1ekbS S: Starting model for refinement |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 12522.299 Da / Num. of mol.: 1 / Fragment: Residues 1-114 (Light chain) / Mutation: N112A Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Production host: Pichia pastoris (fungus) / Strain (production host): KM71 References: UniProt: P05981, Hydrolases; Acting on peptide bonds (peptidases); Serine endopeptidases |
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#2: Protein | Mass: 27573.111 Da / Num. of mol.: 1 / Fragment: Residues 16-255 (Heavy chain) Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Production host: Pichia pastoris (fungus) / Strain (production host): KM71 References: UniProt: P05981, Hydrolases; Acting on peptide bonds (peptidases); Serine endopeptidases |
#3: Chemical | ChemComp-CR4 / |
#4: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.14 Å3/Da / Density % sol: 42.45 % | ||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 291 K / pH: 7.5 Details: ammonium fluoride, PEG 3350, sodium cacodylate, tris, pH 6.2, VAPOR DIFFUSION, HANGING DROP, temperature 291K, pH 7.5, pH 7.50 | ||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 17 ℃ / pH: 7.6 / Method: vapor diffusion, hanging drop | ||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 291 K |
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Diffraction source | Source: ROTATING ANODE / Type: RIGAKU / Wavelength: 1.54 |
Detector | Type: RIGAKU RAXIS IV / Detector: IMAGE PLATE / Date: Oct 9, 2002 / Details: OSMIC MIRRORS |
Radiation | Monochromator: OSMIC MIRRORS / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.54 Å / Relative weight: 1 |
Reflection | Resolution: 1.75→25.7 Å / Num. obs: 30969 / % possible obs: 90.1 % / Observed criterion σ(I): 0 / Redundancy: 3.82 % / Rmerge(I) obs: 0.04 / Net I/σ(I): 12.4 |
Reflection shell | Resolution: 1.75→1.83 Å / Redundancy: 2.11 % / Rmerge(I) obs: 0.261 / Mean I/σ(I) obs: 1.7 / % possible all: 53.7 |
Reflection | *PLUS Highest resolution: 1.75 Å / Lowest resolution: 25.7 Å / Num. obs: 31195 / % possible obs: 96.1 % / Num. measured all: 93729 / Rmerge(I) obs: 0.04 |
Reflection shell | *PLUS % possible obs: 53.3 % / Mean I/σ(I) obs: 1.7 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB ENTRY 1EKB Resolution: 1.75→25.7 Å / Isotropic thermal model: ISOTROPIC / Cross valid method: THROUGHOUT / σ(F): 0.7 / Stereochemistry target values: ENGH & HUBER
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Refinement step | Cycle: LAST / Resolution: 1.75→25.7 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 1.75→1.83 Å /
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Refinement | *PLUS Lowest resolution: 7 Å / Num. reflection Rfree: 3114 / Rfactor Rfree: 0.205 / Rfactor Rwork: 0.187 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS Type: c_bond_d / Dev ideal: 0.018 |