+Open data
-Basic information
Entry | Database: PDB / ID: 1www | ||||||
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Title | NGF IN COMPLEX WITH DOMAIN 5 OF THE TRKA RECEPTOR | ||||||
Components |
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Keywords | NERVE GROWTH FACTOR/TRKA COMPLEX / COMPLEX / TRKA RECEPTOR / NERVE GROWTH FACTOR / CYSTEINE KNOT / IMMUNOGLOBULIN LIKE DOMAIN / NERVE GROWTH FACTOR-TRKA COMPLEX COMPLEX | ||||||
Function / homology | Function and homology information NFG and proNGF binds to p75NTR / Ceramide signalling / nerve growth factor receptor binding / NGF processing / behavioral response to formalin induced pain / neurotrophin p75 receptor binding / olfactory nerve development / response to hydrostatic pressure / TRKA activation by NGF / PLC-gamma1 signalling ...NFG and proNGF binds to p75NTR / Ceramide signalling / nerve growth factor receptor binding / NGF processing / behavioral response to formalin induced pain / neurotrophin p75 receptor binding / olfactory nerve development / response to hydrostatic pressure / TRKA activation by NGF / PLC-gamma1 signalling / programmed cell death involved in cell development / Signalling to STAT3 / p75NTR negatively regulates cell cycle via SC1 / neurotrophin receptor activity / mechanoreceptor differentiation / nerve growth factor receptor activity / metalloendopeptidase inhibitor activity / neurotrophin binding / Sertoli cell development / axonogenesis involved in innervation / GPI-linked ephrin receptor activity / nerve growth factor signaling pathway / nerve development / Retrograde neurotrophin signalling / Axonal growth stimulation / positive regulation of collateral sprouting / nerve growth factor binding / NGF-independant TRKA activation / NADE modulates death signalling / sympathetic nervous system development / Signalling to p38 via RIT and RIN / peripheral nervous system development / ARMS-mediated activation / positive regulation of Ras protein signal transduction / positive regulation of programmed cell death / positive regulation of synapse assembly / PI3K/AKT activation / regulation of neuron differentiation / Frs2-mediated activation / NRAGE signals death through JNK / regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction / detection of temperature stimulus involved in sensory perception of pain / neurotrophin TRK receptor signaling pathway / extrinsic apoptotic signaling pathway via death domain receptors / response to axon injury / neuron development / Signalling to RAS / positive regulation of DNA binding / detection of mechanical stimulus involved in sensory perception of pain / response to electrical stimulus / peptidyl-tyrosine autophosphorylation / cell surface receptor protein tyrosine kinase signaling pathway / p75NTR recruits signalling complexes / positive regulation of neuron differentiation / NF-kB is activated and signals survival / NRIF signals cell death from the nucleus / transmembrane receptor protein tyrosine kinase activity / positive regulation of synaptic transmission, glutamatergic / response to nutrient levels / B cell differentiation / neuron projection morphogenesis / cellular response to nerve growth factor stimulus / positive regulation of GTPase activity / endosome lumen / axon guidance / growth factor activity / modulation of chemical synaptic transmission / receptor protein-tyrosine kinase / memory / kinase binding / positive regulation of neuron projection development / Golgi lumen / cellular response to nicotine / circadian rhythm / peptidyl-tyrosine phosphorylation / recycling endosome membrane / positive regulation of angiogenesis / neuron projection development / synaptic vesicle / late endosome / positive regulation of peptidyl-serine phosphorylation / late endosome membrane / positive regulation of NF-kappaB transcription factor activity / early endosome membrane / protein tyrosine kinase activity / neuron apoptotic process / negative regulation of neuron apoptotic process / protein autophosphorylation / learning or memory / positive regulation of ERK1 and ERK2 cascade / early endosome / receptor complex / endosome membrane / response to xenobiotic stimulus / positive regulation of protein phosphorylation / negative regulation of cell population proliferation / axon / protein phosphorylation / neuronal cell body / lipid binding Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.2 Å | ||||||
Authors | Wiesmann, C. / Ultsch, M.H. / De Vos, A.M. | ||||||
Citation | Journal: Nature / Year: 1999 Title: Crystal structure of nerve growth factor in complex with the ligand-binding domain of the TrkA receptor. Authors: Wiesmann, C. / Ultsch, M.H. / Bass, S.H. / de Vos, A.M. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1www.cif.gz | 99.1 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1www.ent.gz | 75.7 KB | Display | PDB format |
PDBx/mmJSON format | 1www.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1www_validation.pdf.gz | 388.5 KB | Display | wwPDB validaton report |
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Full document | 1www_full_validation.pdf.gz | 406.9 KB | Display | |
Data in XML | 1www_validation.xml.gz | 11.2 KB | Display | |
Data in CIF | 1www_validation.cif.gz | 18.3 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ww/1www ftp://data.pdbj.org/pub/pdb/validation_reports/ww/1www | HTTPS FTP |
-Related structure data
Related structure data | 1betS 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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Noncrystallographic symmetry (NCS) | NCS oper:
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-Components
#1: Protein | Mass: 13515.410 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Production host: Escherichia coli (E. coli) / References: UniProt: P01138 #2: Protein | Mass: 11107.459 Da / Num. of mol.: 2 / Fragment: DOMAIN 5 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Production host: Escherichia coli (E. coli) / References: UniProt: P04629 #3: 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: 2.34 Å3/Da / Density % sol: 47.38 % Description: DATA WERE COLLECTED AT THE ADVANCED LIGHT SOURCE, BERKELEY | ||||||||||||||||||||||||||||||||||||
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Crystal grow | pH: 5 / Details: pH 5.0 | ||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS pH: 8.5 / Method: vapor diffusion, hanging drop | ||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 160 K |
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Diffraction source | Source: SYNCHROTRON / Site: ALS / Beamline: 5.0.2 / Wavelength: 1 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 2.2→20 Å / Num. obs: 23361 / % possible obs: 99.8 % / Redundancy: 4 % / Rsym value: 0.071 / Net I/σ(I): 7.7 |
Reflection shell | Resolution: 2.2→2.28 Å / Redundancy: 3.5 % / Rsym value: 0.355 / % possible all: 98.7 |
Reflection | *PLUS Rmerge(I) obs: 0.071 |
Reflection shell | *PLUS Rmerge(I) obs: 0.355 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 1BET Resolution: 2.2→20 Å / Data cutoff high absF: 10000000 / Data cutoff low absF: 0.001 / Cross valid method: THROUGOUT / σ(F): 0.2
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Refinement step | Cycle: LAST / Resolution: 2.2→20 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.2→2.3 Å / Total num. of bins used: 8
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Software | *PLUS Name: X-PLOR / Version: 3.851 / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Highest resolution: 2.2 Å / Lowest resolution: 20 Å / % reflection Rfree: 10 % / Rfactor obs: 0.189 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS Type: x_angle_deg / Dev ideal: 1.91 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
LS refinement shell | *PLUS Highest resolution: 2.2 Å / Lowest resolution: 2.3 Å / % reflection Rfree: 9.1 % / Rfactor Rwork: 0.283 |