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Yorodumi- PDB-1zwa: STRUCTURE OF HUMAN PARATHYROID HORMONE FRAGMENT 1-34, NMR, 10 STR... -
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Basic information
| Entry | Database: PDB / ID: 1zwa | ||||||
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| Title | STRUCTURE OF HUMAN PARATHYROID HORMONE FRAGMENT 1-34, NMR, 10 STRUCTURES | ||||||
Components | PARATHYROID HORMONE | ||||||
Keywords | HORMONE / DISEASE MUTATION | ||||||
| Function / homology | Function and homology informationmacromolecule biosynthetic process / parathyroid hormone receptor binding / type 1 parathyroid hormone receptor binding / negative regulation of bone mineralization involved in bone maturation / positive regulation of osteoclast proliferation / negative regulation of apoptotic process in bone marrow cell / response to parathyroid hormone / positive regulation of cell proliferation in bone marrow / hormone-mediated apoptotic signaling pathway / magnesium ion homeostasis ...macromolecule biosynthetic process / parathyroid hormone receptor binding / type 1 parathyroid hormone receptor binding / negative regulation of bone mineralization involved in bone maturation / positive regulation of osteoclast proliferation / negative regulation of apoptotic process in bone marrow cell / response to parathyroid hormone / positive regulation of cell proliferation in bone marrow / hormone-mediated apoptotic signaling pathway / magnesium ion homeostasis / positive regulation of signal transduction / response to fibroblast growth factor / cAMP metabolic process / phosphate ion homeostasis / Class B/2 (Secretin family receptors) / negative regulation of chondrocyte differentiation / response to vitamin D / peptide hormone receptor binding / positive regulation of inositol phosphate biosynthetic process / bone mineralization / positive regulation of glycogen biosynthetic process / bone resorption / response to cadmium ion / positive regulation of bone mineralization / Rho protein signal transduction / homeostasis of number of cells within a tissue / skeletal system development / positive regulation of D-glucose import / hormone activity / response to lead ion / adenylate cyclase-activating G protein-coupled receptor signaling pathway / intracellular calcium ion homeostasis / cell-cell signaling / regulation of gene expression / response to ethanol / G alpha (s) signalling events / transcription by RNA polymerase II / G protein-coupled receptor signaling pathway / receptor ligand activity / response to xenobiotic stimulus / negative regulation of gene expression / positive regulation of gene expression / positive regulation of transcription by RNA polymerase II / extracellular space / extracellular region Similarity search - Function | ||||||
| Biological species | Homo sapiens (human) | ||||||
| Method | SOLUTION NMR | ||||||
Authors | Roesch, P. / Marx, U.C. | ||||||
Citation | Journal: Biochem.Biophys.Res.Commun. / Year: 2000Title: Solution structures of human parathyroid hormone fragments hPTH(1-34) and hPTH(1-39) and bovine parathyroid hormone fragment bPTH(1-37). Authors: Marx, U.C. / Adermann, K. / Bayer, P. / Forssmann, W.G. / Rosch, P. #1: Journal: Thesis, University of Bayreuth / Year: 1996Title: Strukturen Verschiedener Parathormonfragmente in Loesung Authors: Marx, U.C. | ||||||
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Structure visualization
| Structure viewer | Molecule: Molmil Jmol/JSmol |
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Downloads & links
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Download
| PDBx/mmCIF format | 1zwa.cif.gz | 119.3 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb1zwa.ent.gz | 96.6 KB | Display | PDB format |
| PDBx/mmJSON format | 1zwa.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 1zwa_validation.pdf.gz | 348.2 KB | Display | wwPDB validaton report |
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| Full document | 1zwa_full_validation.pdf.gz | 405.8 KB | Display | |
| Data in XML | 1zwa_validation.xml.gz | 8.8 KB | Display | |
| Data in CIF | 1zwa_validation.cif.gz | 13.3 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/zw/1zwa ftp://data.pdbj.org/pub/pdb/validation_reports/zw/1zwa | HTTPS FTP |
-Related structure data
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Assembly
| Deposited unit | ![]()
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| 1 |
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| NMR ensembles |
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Components
| #1: Protein/peptide | Mass: 4125.778 Da / Num. of mol.: 1 / Fragment: 1 - 34 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: POTENTIAL / References: UniProt: P01270 |
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-Experimental details
-Experiment
| Experiment | Method: SOLUTION NMR |
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Sample preparation
| Crystal grow | *PLUS Method: other / Details: NMR |
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Processing
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| NMR software | Name: X-PLOR / Version: 3.1 / Developer: BRUNGER / Classification: refinement | ||||||||||||
| NMR ensemble | Conformers submitted total number: 10 |
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