+Open data
-Basic information
Entry | Database: PDB / ID: 2i9b | |||||||||
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Title | Crystal structure of ATF-urokinase receptor complex | |||||||||
Components |
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Keywords | HYDROLASE / urokinase receptor / kringle domain / growth factor-like domain | |||||||||
Function / homology | Function and homology information urokinase plasminogen activator receptor activity / Attachment of GPI anchor to uPAR / positive regulation of homotypic cell-cell adhesion / negative regulation of cysteine-type endopeptidase activity involved in apoptotic signaling pathway / u-plasminogen activator / regulation of smooth muscle cell-matrix adhesion / urokinase plasminogen activator signaling pathway / regulation of plasminogen activation / regulation of fibrinolysis / regulation of wound healing ...urokinase plasminogen activator receptor activity / Attachment of GPI anchor to uPAR / positive regulation of homotypic cell-cell adhesion / negative regulation of cysteine-type endopeptidase activity involved in apoptotic signaling pathway / u-plasminogen activator / regulation of smooth muscle cell-matrix adhesion / urokinase plasminogen activator signaling pathway / regulation of plasminogen activation / regulation of fibrinolysis / regulation of wound healing / protein complex involved in cell-matrix adhesion / regulation of proteolysis / negative regulation of plasminogen activation / regulation of smooth muscle cell migration / regulation of signaling receptor activity / serine-type endopeptidase complex / Dissolution of Fibrin Clot / smooth muscle cell migration / positive regulation of epidermal growth factor receptor signaling pathway / extrinsic component of membrane / plasminogen activation / positive regulation of release of cytochrome c from mitochondria / regulation of cell adhesion mediated by integrin / tertiary granule membrane / positive regulation of DNA binding / negative regulation of fibrinolysis / regulation of cell adhesion / specific granule membrane / negative regulation of intrinsic apoptotic signaling pathway / serine protease inhibitor complex / fibrinolysis / cell projection / chemotaxis / blood coagulation / signaling receptor activity / regulation of cell population proliferation / response to hypoxia / positive regulation of cell migration / positive regulation of protein phosphorylation / protein domain specific binding / endoplasmic reticulum lumen / external side of plasma membrane / serine-type endopeptidase activity / focal adhesion / signaling receptor binding / Neutrophil degranulation / endoplasmic reticulum membrane / negative regulation of apoptotic process / enzyme binding / cell surface / signal transduction / proteolysis / extracellular space / extracellular exosome / extracellular region / membrane / plasma membrane Similarity search - Function | |||||||||
Biological species | Homo sapiens (human) | |||||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.8 Å | |||||||||
Authors | Lubkowski, J. / Barinka, C. | |||||||||
Citation | Journal: J.Mol.Biol. / Year: 2006 Title: Structural basis of interaction between urokinase-type plasminogen activator and its receptor. Authors: Barinka, C. / Parry, G. / Callahan, J. / Shaw, D.E. / Kuo, A. / Bdeir, K. / Cines, D.B. / Mazar, A. / Lubkowski, J. | |||||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2i9b.cif.gz | 307.4 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2i9b.ent.gz | 248.2 KB | Display | PDB format |
PDBx/mmJSON format | 2i9b.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 2i9b_validation.pdf.gz | 1.6 MB | Display | wwPDB validaton report |
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Full document | 2i9b_full_validation.pdf.gz | 1.7 MB | Display | |
Data in XML | 2i9b_validation.xml.gz | 58.4 KB | Display | |
Data in CIF | 2i9b_validation.cif.gz | 78.1 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/i9/2i9b ftp://data.pdbj.org/pub/pdb/validation_reports/i9/2i9b | HTTPS FTP |
-Related structure data
Related structure data | 2i9aSC 1ywhS S: Starting model for refinement C: citing same article (ref.) |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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Unit cell |
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Noncrystallographic symmetry (NCS) | NCS domain:
NCS domain segments: Component-ID: 1 / Refine code: 1
NCS ensembles :
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Details | The biological unit is a heterodimer of ligand (ATF) and the receptor (uPAR). There are 4 biological units in the asymmetric unit. |
-Components
-Protein , 2 types, 8 molecules ABCDEFGH
#1: Protein | Mass: 16398.461 Da / Num. of mol.: 4 / Fragment: ATF, residues 21-163 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: PLAU / Plasmid: pMT/BiP/V5-His / Production host: Drosophila melanogaster (fruit fly) / Strain (production host): Schneider's S2 cells / References: UniProt: P00749, u-plasminogen activator #2: Protein | Mass: 31109.963 Da / Num. of mol.: 4 / Fragment: UPAR, residues 23-299 / Mutation: N162Q, N172Q, N200Q, N233Q Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: PLAUR, MO3, UPAR / Plasmid: pMT/BiP/V5-His / Production host: Drosophila melanogaster (fruit fly) / Strain (production host): Schneider's S2 cells / References: UniProt: Q03405 |
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-Sugars , 2 types, 4 molecules
#3: Polysaccharide | Source method: isolated from a genetically manipulated source #4: Polysaccharide | Source method: isolated from a genetically manipulated source |
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-Non-polymers , 2 types, 54 molecules
#5: Chemical | #6: Water | ChemComp-HOH / | |
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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: 2.82 Å3/Da / Density % sol: 56.46 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 5.5 Details: 22.5% w/v PEG3350, 200 mM ammonium sulfate, 100 mM Bis-Tris, pH 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: APS / Beamline: 22-BM / Wavelength: 1 Å |
Detector | Type: MAR CCD 225 mm / Detector: CCD / Date: Jul 7, 2005 |
Radiation | Monochromator: Crystal / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 2.8→50 Å / Num. all: 47048 / Num. obs: 47048 / % possible obs: 91.2 % / Observed criterion σ(I): -3 / Redundancy: 2.8 % / Rsym value: 0.046 / Net I/σ(I): 17.6 |
Reflection shell | Resolution: 2.8→2.9 Å / Redundancy: 1.8 % / Mean I/σ(I) obs: 2.44 / Num. unique all: 2636 / Rsym value: 0.206 / % possible all: 51.3 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB ENTRY 1YWH, 2I9A Resolution: 2.8→15 Å / Cor.coef. Fo:Fc: 0.928 / Cor.coef. Fo:Fc free: 0.899 / SU B: 30.164 / SU ML: 0.284 / TLS residual ADP flag: LIKELY RESIDUAL / Cross valid method: THROUGHOUT / ESU R Free: 0.398 / Stereochemistry target values: MAXIMUM LIKELIHOOD
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 67.301 Å2
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Refinement step | Cycle: LAST / Resolution: 2.8→15 Å
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Refine LS restraints |
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Refine LS restraints NCS | Dom-ID: 1 / Refine-ID: X-RAY DIFFRACTION
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LS refinement shell | Resolution: 2.801→2.872 Å / Total num. of bins used: 20
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Refinement TLS params. | Method: refined / Refine-ID: X-RAY DIFFRACTION
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Refinement TLS group |
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