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Open data
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Basic information
Entry | Database: PDB / ID: 1hgu | ||||||
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Title | HUMAN GROWTH HORMONE | ||||||
![]() | HUMAN GROWTH HORMONE | ||||||
![]() | HORMONE | ||||||
Function / homology | ![]() growth hormone activity / growth hormone receptor complex / bone maturation / prolactin receptor binding / positive regulation of growth / animal organ development / positive regulation of activation of Janus kinase activity / positive regulation of multicellular organism growth / positive regulation of glucose transmembrane transport / positive regulation of insulin-like growth factor receptor signaling pathway ...growth hormone activity / growth hormone receptor complex / bone maturation / prolactin receptor binding / positive regulation of growth / animal organ development / positive regulation of activation of Janus kinase activity / positive regulation of multicellular organism growth / positive regulation of glucose transmembrane transport / positive regulation of insulin-like growth factor receptor signaling pathway / growth hormone receptor binding / growth hormone receptor signaling pathway / Prolactin receptor signaling / cell surface receptor signaling pathway via JAK-STAT / Synthesis, secretion, and deacylation of Ghrelin / Growth hormone receptor signaling / positive regulation of tyrosine phosphorylation of STAT protein / response to nutrient levels / cytokine activity / endosome lumen / positive regulation of receptor signaling pathway via JAK-STAT / positive regulation of MAP kinase activity / growth factor activity / hormone activity / cytokine-mediated signaling pathway / response to estradiol / positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction / extracellular space / extracellular region / metal ion binding Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() | ||||||
![]() | Chantalat, L. / Jones, N. / Korber, F. / Navaza, J. / Pavlovsky, A.G. | ||||||
![]() | Journal: Protein Pept.Lett. / Year: 1995 Title: THE CRYSTAL-STRUCTURE OF WILD-TYPE GROWTH-HORMONE AT 2.5 ANGSTROM RESOLUTION. Authors: Chantalat, L. / Jones, N.D. / Korber, F. / Navaza, J. / Pavlovsky, A.G. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 48.5 KB | Display | ![]() |
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PDB format | ![]() | 38.7 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 396.4 KB | Display | ![]() |
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Full document | ![]() | 424.6 KB | Display | |
Data in XML | ![]() | 9.7 KB | Display | |
Data in CIF | ![]() | 13 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: CIS PROLINE - PRO 37 2: ALA 67 - GLN 68 OMEGA = 215.88 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION 3: GLN 68 - GLN 69 OMEGA = 226.17 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION 4: ASP 107 - SER 108 OMEGA = 238.99 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION 5: SER 108 - ASP 109 OMEGA = 269.60 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION 6: ASN 149 - SER 150 OMEGA = 137.02 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION 7: ASP 153 - ASP 154 OMEGA = 141.53 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION |
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Components
#1: Protein | Mass: 21902.771 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
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#2: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.41 Å3/Da / Density % sol: 49.04 % | |||||||||||||||||||||||||
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Crystal grow | *PLUS pH: 7 / Method: vapor diffusion, hanging drop | |||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction source | Wavelength: 1.5418 |
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Detector | Type: SIEMENS / Detector: AREA DETECTOR |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Rmerge(I) obs: 0.0747 |
Reflection | *PLUS Highest resolution: 2.5 Å / Lowest resolution: 15 Å / Num. obs: 5364 / % possible obs: 66.6 % / Num. measured all: 13055 / Rmerge(I) obs: 0.0747 |
Reflection shell | *PLUS Highest resolution: 2.5 Å / Lowest resolution: 2.75 Å / % possible obs: 37.1 % |
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Processing
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Refinement | Rfactor Rwork: 0.212 / Rfactor obs: 0.212 / Highest resolution: 2.5 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 34 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine analyze | Luzzati coordinate error obs: 0.32 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Highest resolution: 2.5 Å
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Refine LS restraints |
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Software | *PLUS Name: X-PLOR/PROLSQ / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Lowest resolution: 8 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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