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- PDB-3hhr: HUMAN GROWTH HORMONE AND EXTRACELLULAR DOMAIN OF ITS RECEPTOR: CR... -
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Open data
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Basic information
Entry | Database: PDB / ID: 3hhr | |||||||||
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Title | HUMAN GROWTH HORMONE AND EXTRACELLULAR DOMAIN OF ITS RECEPTOR: CRYSTAL STRUCTURE OF THE COMPLEX | |||||||||
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![]() | HORMONE/RECEPTOR / HORMONE-RECEPTOR complex | |||||||||
Function / homology | ![]() growth hormone receptor activity / regulation of response to nutrient levels / growth hormone activity / growth hormone receptor complex / bone maturation / prolactin receptor binding / positive regulation of growth / taurine metabolic process / animal organ development / positive regulation of activation of Janus kinase activity ...growth hormone receptor activity / regulation of response to nutrient levels / growth hormone activity / growth hormone receptor complex / bone maturation / prolactin receptor binding / positive regulation of growth / taurine metabolic process / animal organ development / positive regulation of activation of Janus kinase activity / response to gravity / cartilage development involved in endochondral bone morphogenesis / positive regulation of multicellular organism growth / hormone metabolic process / positive regulation of glucose transmembrane transport / proline-rich region binding / positive regulation of insulin-like growth factor receptor signaling pathway / growth hormone receptor binding / response to food / growth hormone receptor signaling pathway / response to cycloheximide / cytokine binding / Prolactin receptor signaling / growth factor binding / cell surface receptor signaling pathway via JAK-STAT / peptide hormone binding / regulation of multicellular organism growth / Synthesis, secretion, and deacylation of Ghrelin / Growth hormone receptor signaling / response to glucocorticoid / positive regulation of tyrosine phosphorylation of STAT protein / cellular response to hormone stimulus / hormone-mediated signaling pathway / response to interleukin-1 / SH2 domain binding / response to nutrient levels / insulin-like growth factor receptor signaling pathway / cytokine activity / endosome lumen / positive regulation of cell differentiation / positive regulation of receptor signaling pathway via JAK-STAT / growth factor activity / positive regulation of MAP kinase activity / hormone activity / receptor internalization / cytokine-mediated signaling pathway / cytoplasmic ribonucleoprotein granule / endocytosis / cellular response to insulin stimulus / positive regulation of peptidyl-tyrosine phosphorylation / response to estradiol / protein phosphatase binding / positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction / receptor complex / external side of plasma membrane / neuronal cell body / lipid binding / protein kinase binding / cell surface / protein homodimerization activity / extracellular space / extracellular region / identical protein binding / membrane / metal ion binding / plasma membrane / cytosol Similarity search - Function | |||||||||
Biological species | ![]() | |||||||||
Method | ![]() | |||||||||
![]() | De Vos, A.M. / Ultsch, M. / Kossiakoff, A.A. | |||||||||
![]() | ![]() Title: Human growth hormone and extracellular domain of its receptor: crystal structure of the complex. Authors: de Vos, A.M. / Ultsch, M. / Kossiakoff, A.A. #1: ![]() Title: Crystals of the Complex between Human Growth Hormone and the Extracellular Domain of its Receptor Authors: Ultsch, M. / De Vos, A.M. / Kossiakoff, A.A. #2: ![]() Title: Dimerization of the Extracellular Domain of the Human Growth Hormone Receptor by a Single Hormone Molecule Authors: Cunningham, B.C. / Ultsch, M. / De Vos, A.M. / Mulkerrin, M.G. / Clauser, K.R. / Wells, J.A. | |||||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 123.6 KB | Display | ![]() |
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PDB format | ![]() | 96.5 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 383.9 KB | Display | ![]() |
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Full document | ![]() | 405.5 KB | Display | |
Data in XML | ![]() | 14.4 KB | Display | |
Data in CIF | ![]() | 21.4 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
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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Atom site foot note | 1: ASP B 52 - GLU B 53 OMEGA =220.92 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION 2: GLU B 53 - VAL B 54 OMEGA =214.97 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION 3: LEU B 233 - PRO B 234 OMEGA = 31.98 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION 4: GLY C 62 - PRO C 63 OMEGA =149.08 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION |
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Components
#1: Protein | Mass: 22004.818 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() |
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#2: Protein | Mass: 24004.004 Da / Num. of mol.: 2 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: 2.71 Å3/Da / Density % sol: 54.66 % | |||||||||||||||||||||||||||||||||||
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Crystal grow | *PLUS pH: 7.5 / Method: vapor diffusion, hanging drop / Details: referred to J.Mol.Biol. 222.865-868 | |||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Reflection | *PLUS Highest resolution: 2.8 Å / Lowest resolution: 15 Å / Rmerge(I) obs: 0.204 |
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Processing
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Refinement | Rfactor Rwork: 0.221 / Rfactor obs: 0.221 / Highest resolution: 2.8 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Highest resolution: 2.8 Å
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Refine LS restraints |
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Software | *PLUS Name: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Rfactor obs: 0.221 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS Type: x_angle_d / Dev ideal: 3.2 |