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Yorodumi- PDB-1zwf: STRUCTURE OF N-TERMINAL ACETYLATED HUMAN PARATHYROID HORMONE, NMR... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1zwf | ||||||
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Title | STRUCTURE OF N-TERMINAL ACETYLATED HUMAN PARATHYROID HORMONE, NMR, 10 STRUCTURES | ||||||
Components | PARATHYROID HORMONE | ||||||
Keywords | HORMONE / DISEASE MUTATION | ||||||
Function / homology | Function and homology information parathyroid hormone receptor binding / type 1 parathyroid hormone receptor binding / negative regulation of bone mineralization involved in bone maturation / negative regulation of apoptotic process in bone marrow cell / positive regulation of osteoclast proliferation / response to parathyroid hormone / macromolecule biosynthetic process / hormone-mediated apoptotic signaling pathway / positive regulation of cell proliferation in bone marrow / positive regulation of signal transduction ...parathyroid hormone receptor binding / type 1 parathyroid hormone receptor binding / negative regulation of bone mineralization involved in bone maturation / negative regulation of apoptotic process in bone marrow cell / positive regulation of osteoclast proliferation / response to parathyroid hormone / macromolecule biosynthetic process / hormone-mediated apoptotic signaling pathway / positive regulation of cell proliferation in bone marrow / positive regulation of signal transduction / magnesium ion homeostasis / response to fibroblast growth factor / phosphate ion homeostasis / cAMP metabolic process / response to vitamin D / negative regulation of chondrocyte differentiation / Class B/2 (Secretin family receptors) / positive regulation of inositol phosphate biosynthetic process / peptide hormone receptor binding / bone mineralization / Rho protein signal transduction / positive regulation of glycogen biosynthetic process / bone resorption / positive regulation of bone mineralization / response to cadmium ion / homeostasis of number of cells within a tissue / skeletal system development / positive regulation of D-glucose import / response to lead ion / adenylate cyclase-activating G protein-coupled receptor signaling pathway / hormone activity / intracellular calcium ion homeostasis / cell-cell signaling / regulation of gene expression / G alpha (s) signalling events / response to ethanol / transcription by RNA polymerase II / receptor ligand activity / response to xenobiotic stimulus / G protein-coupled receptor signaling pathway / 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: Strukturen Verschiedener Parathormonfragmente in Loesung Year: 1996 Authors: Marx, U.C. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1zwf.cif.gz | 122.4 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1zwf.ent.gz | 98.7 KB | Display | PDB format |
PDBx/mmJSON format | 1zwf.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1zwf_validation.pdf.gz | 352.3 KB | Display | wwPDB validaton report |
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Full document | 1zwf_full_validation.pdf.gz | 414.8 KB | Display | |
Data in XML | 1zwf_validation.xml.gz | 9 KB | Display | |
Data in CIF | 1zwf_validation.cif.gz | 13.6 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/zw/1zwf ftp://data.pdbj.org/pub/pdb/validation_reports/zw/1zwf | HTTPS FTP |
-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein/peptide | Mass: 4161.896 Da / Num. of mol.: 1 / Fragment: 4 - 37 / Mutation: N-TERMINAL ACETYLATED Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: POTENTIAL / References: UniProt: P01270 |
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Has protein modification | Y |
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR |
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-Processing
Software |
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NMR software | Name: X-PLOR / Version: 3.1 / Developer: BRUNGER / Classification: refinement | ||||||||||||
NMR ensemble | Conformers submitted total number: 10 |