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- PDB-2uzy: Structure of the human receptor tyrosine kinase Met in complex wi... -
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Open data
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Basic information
Entry | Database: PDB / ID: 2uzy | ||||||
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Title | Structure of the human receptor tyrosine kinase Met in complex with the Listeria monocytogenes invasion protein inlb: low resolution, Crystal form II | ||||||
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Function / homology | ![]() negative regulation of guanyl-nucleotide exchange factor activity / ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() Similarity search - Function | ||||||
Biological species | ![]() ![]() ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Niemann, H.H. / Jager, V. / Butler, P.J.G. / van den Heuvel, J. / Schmidt, S. / Ferraris, D. / Gherardi, E. / Heinz, D.W. | ||||||
![]() | ![]() Title: Structure of the Human Receptor Tyrosine Kinase met in Complex with the Listeria Invasion Protein Inlb Authors: Niemann, H.H. / Jager, V. / Butler, P.J.G. / van den Heuvel, J. / Schmidt, S. / Ferraris, D. / Gherardi, E. / Heinz, D.W. | ||||||
History |
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Remark 700 | SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN ... SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW, TWO SHEETS ARE DEFINED. |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 371.2 KB | Display | ![]() |
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PDB format | ![]() | 294.9 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 2uzxC ![]() 1h6tS ![]() 1shyS 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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1 | ![]()
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2 | ![]()
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Unit cell |
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Noncrystallographic symmetry (NCS) | NCS oper:
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Components
#1: Protein | Mass: 32243.818 Da / Num. of mol.: 2 Fragment: INTERNALIN DOMAIN (CAP, LRR, IR)\: INLB321, RESIDUES 36-321 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() ![]() #2: Protein | ![]() Mass: 81903.047 Da / Num. of mol.: 2 / Fragment: SEMA, PSI, IG1, IG2\: MET741, RESIDUES 25-740 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() ![]() Compound details | MEDIATES THE ENTRY OF LISTERIA MONOCYTOGENES INTO CELLS. RECEPTOR FOR HEPATOCYTE GROWTH FACTOR AND ...MEDIATES THE ENTRY OF LISTERIA MONOCYTOGE | Sequence details | CHAIN A+C: RESIDUES 33-35 (GAM) REMAIN AFTER TEV CLEAVAGE CHAIN B+D: Y41C AND G344A PROBABLY DUE TO ...CHAIN A+C: RESIDUES 33-35 (GAM) REMAIN AFTER TEV CLEAVAGE CHAIN B+D: Y41C AND G344A PROBABLY DUE TO PCR ERROR. N-TERMINAL ETR LEFT AFTER PROCESSING | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 3.33 Å3/Da / Density % sol: 63 % / Description: NONE |
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Crystal grow![]() | Temperature: 298 K / Method: vapor diffusion, sitting drop Details: VAPOR DIFFUSION AT 25 DEGREE C IN SITTING-DROPS. 2 UL PROTEIN (8 MG/ML)PLUS 2 UL RESERVOIR (1.4 M NA/K PHOSPHATE, PH 6.5, 10% PEG 2000 MONO-METHYL-ETHER) |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: MARRESEARCH / Detector: CCD / Date: May 19, 2006 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength![]() |
Reflection | Resolution: 4→20 Å / Num. obs: 26274 / % possible obs: 99.5 % / Observed criterion σ(I): -3 / Redundancy: 9.6 % / Rmerge(I) obs: 0.22 / Net I/σ(I): 5.99 |
Reflection shell | Resolution: 4→4.1 Å / Redundancy: 9.8 % / Rmerge(I) obs: 0.57 / Mean I/σ(I) obs: 2.21 / % possible all: 99.9 |
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Processing
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Refinement | Method to determine structure![]() ![]() Starting model: PDB ENTRIES 1H6T, 1SHY Resolution: 4→15 Å Details: B-FACTORS MODELED SOLELY BY TLS. TOTAL ISOTROPIC B-FACTORS GIVEN. TIGHT NCS ON INDIVIDUAL DOMAINS EMPLOYED THROUGHOUT.
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Refinement step | Cycle: LAST / Resolution: 4→15 Å
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