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Open data
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Basic information
Entry | Database: PDB / ID: 6wmw | ||||||
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Title | GFRAL receptor bound with two antibody Fabs (3P10, 25M22) | ||||||
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Function / homology | ![]() GDF15-GFRAL signaling pathway / response to metformin / reduction of food intake in response to dietary excess / glial cell-derived neurotrophic factor receptor activity / glial cell-derived neurotrophic factor receptor signaling pathway / negative regulation of appetite / stress-activated protein kinase signaling cascade / negative regulation of extrinsic apoptotic signaling pathway in absence of ligand / ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | White, A. / Lakshminarasimhan, D. / Olland, A. / Suto, R.K. | ||||||
![]() | ![]() Title: Antibody-mediated inhibition of GDF15-GFRAL activity reverses cancer cachexia in mice. Authors: Suriben, R. / Chen, M. / Higbee, J. / Oeffinger, J. / Ventura, R. / Li, B. / Mondal, K. / Gao, Z. / Ayupova, D. / Taskar, P. / Li, D. / Starck, S.R. / Chen, H.H. / McEntee, M. / Katewa, S.D. ...Authors: Suriben, R. / Chen, M. / Higbee, J. / Oeffinger, J. / Ventura, R. / Li, B. / Mondal, K. / Gao, Z. / Ayupova, D. / Taskar, P. / Li, D. / Starck, S.R. / Chen, H.H. / McEntee, M. / Katewa, S.D. / Phung, V. / Wang, M. / Kekatpure, A. / Lakshminarasimhan, D. / White, A. / Olland, A. / Haldankar, R. / Solloway, M.J. / Hsu, J.Y. / Wang, Y. / Tang, J. / Lindhout, D.A. / Allan, B.B. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 218.6 KB | Display | ![]() |
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PDB format | ![]() | 171.5 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 5vz4S S: Starting model for refinement |
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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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Unit cell |
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Components
#1: Protein | ![]() Mass: 27665.693 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() ![]() |
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#2: Antibody | Mass: 24098.934 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() |
#3: Antibody | Mass: 23745.457 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() |
#4: Antibody | Mass: 24894.943 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() |
#5: Antibody | Mass: 26652.068 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.72 Å3/Da / Density % sol: 54.81 % |
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Crystal grow![]() | Temperature: 297 K / Method: vapor diffusion, sitting drop / pH: 7 / Details: 0.1 M IMIDAZOLE Ph 7.0 AND 12% (w/w) peg 20,000 |
-Data collection
Diffraction | Mean temperature: 100 K / Serial crystal experiment: N | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Diffraction source | Source: ![]() ![]() ![]() | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Detector | Type: ADSC QUANTUM 315r / Detector: CCD / Date: Jan 23, 2016 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Radiation wavelength | Wavelength![]() | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Reflection | Resolution: 2.9→50 Å / Num. obs: 31586 / % possible obs: 99.6 % / Redundancy: 6.6 % / Rmerge(I) obs: 0.099 / Rpim(I) all: 0.041 / Rrim(I) all: 0.108 / Χ2: 0.996 / Net I/σ(I): 10.2 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Reflection shell | Diffraction-ID: 1
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Processing
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Refinement | Method to determine structure![]() ![]() Starting model: 5vz4 Resolution: 2.91→47.7 Å / Cor.coef. Fo:Fc: 0.926 / Cor.coef. Fo:Fc free: 0.876 / SU B: 20.882 / SU ML: 0.39 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R Free: 0.446 Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS U VALUES : REFINED INDIVIDUALLY
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso max: 209.9 Å2 / Biso mean: 75.054 Å2 / Biso min: 26.28 Å2
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Refinement step | Cycle: final / Resolution: 2.91→47.7 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.9→2.975 Å / Rfactor Rfree error: 0 / Total num. of bins used: 20
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